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Synthesis, conformational analysis and biological activity of cyclic analogs of the octadecaneuropeptide ODN Design of a potent endozepine antagonist Je´roˆme Leprince1, Hassan Oulyadi2,

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Synthesis, conformational analysis and biological activity of cyclic analogs of the octadecaneuropeptide ODN

Design of a potent endozepine antagonist

Je´roˆme Leprince1, Hassan Oulyadi2, David Vaudry1, Olfa Masmoudi1, Pierrick Gandolfo1, Christine Patte1, Jean Costentin3, Jean-Luc Fauche`re4, Daniel Davoust2, Hubert Vaudry1and Marie-Christine Tonon1

1 Institut Fe´de´ratif de Recherches Multidisciplinaires sur les Peptides (IFRMP 23), Laboratoire de Neuroendocrinologie Cellulaire et Mole´culaire, Institut National de la Sante´ et de la Recherche Me´dicale Unite´ 413, CNRS, Universite´ de Rouen, Mont-Saint-Aignan, France;

2 IFRMP 23, Laboratoire de Re´sonance Magne´tique Nucle´aire, Institut de Recherche en Chimie Organique Fine, CNRS Unite´ Mixte de Recherches 6014, Universite´ de Rouen, Mont-Saint-Aignan, France;3IFRMP 23, Laboratoire de Neuropsychopharmacologie, CNRS Unite´ Mixte de Recherches 6036, Universite´ de Rouen, Rouen, France; 4 Institut de Recherches SERVIER, Suresnes, France

The octadecaneuropeptide (ODN; QATVGDVNTDRPG

LLDLK) and its C-terminal octapeptide (OP; RPGLLDLK),

which exert anxiogenic activity, have been previously shown

to increase intracellular calcium concentration ([Ca21]i) in

cultured rat astrocytes through activation of a metabotropic

receptor positively coupled to phospholipase C It has also

been found that the [D-Leu5]OP analog possesses a weak

antagonistic activity The aim of the present study was to

synthesize and characterize cyclic analogs of OP and

[D-Leu5]OP On-resin homodetic backbone cyclization of

OP yielded an analog, cyclo128OP, which was three times

more potent and 1.4-times more efficacious than OP to

increase [Ca21]iin cultured rat astrocytes Cyclo128OP also

mimicked the effect of both OP and ODN on

polyphos-phoinositide turnover Conversely, the cyclo128[D-Leu5]OP

analog was totally devoid of agonistic activity but

suppressed the effect of OP and ODN on [Ca21]i and phosphoinositide metabolism in astrocytes The structure of these cyclic analogs has been determined by two-dimen-sional 1H-NMR and molecular dynamics Cyclo128 OP exhibited a single conformation characterized by a g turn comprising residues Pro2 – Leu4 and a type III b turn encompassing residues Leu5 – Lys8 Cyclo128[D-Leu5]OP was present as two equimolar conformers resulting from cis/trans isomerization of the Arg – Pro peptide bond These pharmacological and structural data should prove useful for the rational design of non peptidic ODN analogs

Keywords: solid-phase peptide synthesis; cyclic peptides; structure-activity relationship; astrocytes; cytosolic calcium concentration

Diazepam-binding inhibitor (DBI) is an 86-amino-acid

polypeptide that has been originally isolated from rat brain

extracts as an endogenous ligand of benzodiazepine (BZ)

receptors [1] Proteolytic cleavage of DBI generates several biologically active peptides including the triakontatetra-neuropeptide TTN (DBI17250) [2] and the octadecaneuro-peptide ODN (DBI33250) [3] which are collectively designated by the term endozepines [4] Intracerebroven-tricular injection of endozepines provokes anxiogenic effects [5], induces proconflict behavior [1,6], reverses the anti-conflict action of diazepam [1] and inhibits food intake [7] The mechanism of action of endozepines is not fully understood It has been initially proposed that these peptides act as inverse agonists of central-type benzodiazepine receptors [6] thus inhibiting the activity of the GABAA -chloride channel complex [8] Subsequently, endozepines were found to interact with peripheral-type BZ receptors and

to stimulate cholesterol transport into mitochondria [9] More recently, it has been shown that, in rat astrocytes, ODN activates a metabotropic receptor positively coupled to phospholipase C, leading to an increase in cytosolic calcium concentration [10,11] Structure-activity relation-ship studies have shown that the C-terminal octapeptide of ODN (OP; ODN11218) is the minimum sequence retaining full calcium-mobilizing activity [12] The Ala-scan of OP has revealed that replacement of the Leu6 residue suppresses the activity of the peptide It has also been found that the [D-Leu5]OP analog exhibits a weak antagonistic activity [12]

Correspondence to H Vaudry, European Institute for Peptide Research,

Laboratory of Cellular and Molecular Neuroendocrinology, Institut

National de la Sante´ et de la Recherche Me´dicale Unite´ 413, Unite´

Associe´e au Centre National de la Recherche Scientifique, University of

Rouen, 76821 Mont-Saint-Aignan, France Fax: 1 33 235 14 6946,

Tel.: 1 33 235 14 6624, E-mail: hubert.vaudry@univ-rouen.fr

Note: all optically active amino acids are of the L configuration unless

otherwise noted.

(Received 17 April 2001, revised 30 July 2001, accepted 21 September

2001)

Abbreviations: ODN, octadecaneuropeptide; OP, octapeptide; DBI,

diazepam-binding inhibitor; BZ, benzodiazepine; TTN,

triakontatetraneuropeptide; HMP,

4-hydroxymethyl-phenoxymethyl-copolystyrene-1%-divinylbenzene resin; HBTU,

O-benzotriazol-1-yl-N,N,N 0 ,N 0 -tetramethyluronium hexafluorophosphate; HOBt,

1-hydroxybenzotriazole; DIEA, N,N-diisopropylethylamine; PEG-PS,

poly(ethylene glycol) – polystyrene resin; NMP,

N-methylpyrrolidin-2-one; DMF, N,N-dimethylformamide; [Ph 3 P] 4 Pd,

tetrakis(triphenylphosphine)palladium(0); NMM,

N-methylmorpholine; DMEM, Dulbecco’s modified Eagle’s medium;

DSS, sodium 2,2-dimethyl-2-silapentane-5-sulfonate; IP, inositol

phosphate; PIP, polyphosphoinositide.

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On the basis of these observations, we have undertaken

the design of selective ODN analogs that would exhibit high

affinity for the rat astrocyte endozepine receptor Backbone

cyclization is an efficient approach which has been widely

used to stabilize the spatial conformation of peptides

without altering the side chain motifs that are often involved

in their biological activity [13,14] In several cases,

cycliz-ation has been found to enhance the potency of peptides on

their receptors [15 – 18] The aim of the present study was

to prepare head-to-tail cyclic analogs of OP in order to

generate possible agonists and antagonists of ODN We have

determined the secondary structure of the cyclic OP analogs

by two-dimensional 1H-NMR and molecular dynamic

simulation, and we have investigated the biological activity

of these analogs by measuring their ability to modify

cytosolic calcium concentrations and polyphosphoinositide

turnover in cultured rat astrocytes

M A T E R I A L S A N D M E T H O D S

Materials

All amino-acid residues, preloaded

4-hydroxymethyl-phenoxymethyl-copolystyrene-1%-divinylbenzene resin

[Fmoc-Lys(Boc)-HMP], O-benzotriazol-1-yl-N,N,N0,N0

-tetramethyluronium hexafluorophosphate (HBTU),

1-hydroxybenzotriazole (HOBt), piperidine and

N,N-diiso-propylethylamine (DIEA) were purchased from Applied

Biosystems (St Quentin en Yvelines, France) Preloaded poly

(ethylene glycol) –polystyrene resin

[Fmoc-Asp(PEG-PS)-OAl] was obtained from PerSeptive Biosystems

(Voisins-le-Bretonneux, France) Trifluoroacetic acid, trichloroacetic

acid, phenol, thioanisol, ethanedithiol,

N-methylpyrrolidin-2-one (NMP), N,N-dimethylformamide (DMF), tetrakis

(triphenylphosphine)palladium(0) ([Ph3P]4Pd), sodium

diethyldithiocarbamate, N-methylmorpholine (NMM),

U73122

(1-[6-([(17b)-3-methoxyestra-1,3,5-(10)-trien-17-yl]amino)hexyl]1H-pyrrole-2,5-dione), Dulbecco’s

modified Eagle’s medium (DMEM), F12 culture medium,

insulin andD(1)-glucose were from Sigma-Aldrich Chimie

(St Quentin Fallavier, France) Glutamine, the antibiotic –

antimycotic solution and Hepes were from Bioproducts

(Gagny, France) Fetal bovine serum was from Biosys

(Compie`gne, France) BSA (fraction V) was from Roche

Molecular Biochemicals (Mannheim, Germany)

Indo-1-acetoxymethyl ester and fluo-4-Indo-1-acetoxymethyl ester were

from Molecular Probes Europe (Leiden, The Netherlands)

Myo-[3H]inositol (100 Ci:mmol21) was from Amersham

International (Les Ulis, France) Sodium

2,2-dimethyl-2-silapentane-5-sulfonate (DSS) and D2O were from

Euriso-top (CEA, Saclay, France)

Peptide synthesis

ODN (QATVGDVNTDRPGLLDLK) and OP (RPGLLDLK)

were synthesized (0.25 mmol scale for ODN; 0.1 mmol

scales for OP) on a Fmoc-Lys(Boc)-HMP resin using an

Applied Biosystems model 433A peptide synthesizer using

the standard FastMocVMonPrevPKw procedure as

pre-viously described [12] The synthesis of linear precursors of

cyclo128OP and cyclo128[D-Leu5]OP (0.25 mmol scale

each) was performed on a PioneerTMPerSeptive Biosystems

peptide synthesizer on a Fmoc-Asp(PEG-PS)-OAl resin

using similar coupling procedure, extended to a capping cycle of the nonacylated primary amine After completion

of the chain assembly, deprotection of the allyl ester was performed manually by Pd(0) under Ar as previously described [19,20] The catalyst (3 eq., 0.75 mmol), dis-solved in 26 mL Ac2O/CHCl3/NMM mixture (2 : 37 : 1; v/v/v) was transferred to a sealed tube containing the Fmoc-peptidyl(resin)-OAl using an Ar flushed gas-tight syringe and gently agitated for 2.5 h at room temperature The resin was then washed sequentially with fresh catalyst dissolving mixture, 0.5% DIEA in DMF, 0.5% sodium diethyldithio-carbamate in DMF, 0.5% HOBt in DMF and DCM, and dried in vacuo The N-terminal Fmoc group was removed by treatment with 20% piperidine in NMP Prior to each manual step, part of the X-peptidyl(resin)-Y (X ¼ Fmoc or H;

Y ¼ OAl or OH) was completely deprotected by trifluoro-acetic acid to generate linear peptide sequences for reversed-phase HPLC (RP-HPLC) analysis On-resin head-to-tail cyclization of the peptide was performed twice by addition

of HBTU/DIEA (8 eq., 2 mmol; 1 : 1, mol/mol) in 15 mL

of DMF for 2  3.5 h with occasional gentle agitation Cyclization was monitored by the Kaiser’s test Peptides were deprotected and cleaved from the resin as previously described [12]

Peptide purification All peptides were purified by RP-HPLC on a semiprepara-tive Vydac C18column (1  25 cm; Touzart et Matignon, Courtaboeuf, France) using a linear gradient (10 – 50% over

40 min) of acetonitrile/trifluoroacetic acid (99.9 : 0.1, v/v)

at a flow rate of 5 mL:min21 Analytical RP-HPLC was performed on a Vydac C18column (0.45  25 cm) using a linear gradient (10 – 40% over 30 min) of acetonitrile/ trifluoroacetic acid at a flow rate of 1 mL:min21 The purified peptides were characterized by FAB-MS on a conventional EB geometry mass spectrometer JEOL model AX-500 equipped with a DEC data system (JEOL-Europe

SA, Croissy-sur-Seine, France) or by MALDI-TOF-MS on a Tofspec E (Micromass, Manchester, UK)

Cell culture Primary cultures of rat astrocytes were performed as pre-viously described [21] Briefly, cerebral hemispheres from newborn Wistar rats were collected in DMEM/F12 culture medium (2 : 1, v/v) supplemented with 2 mM glutamine, 1% insulin, 5 mMHepes, 0.4%D(1)-glucose and 1% of the antibiotic/antimicotic solution The tissues were disaggre-gated mechanically using a Pasteur pipette, and filtered through a 100-mm nylon sieve (Poly Labo, Strasbourg, France) Dissociated cells were resuspended in culture medium supplemented with 10% fetal bovine serum and seeded on coverslips in 35-mm dishes (Dutscher, Brumath, France) at a density of 106cells per dish The cells were incubated at 37 8C in a moist atmosphere (5% CO2), and the medium was changed twice a week

Confocal imaging Five- to seven-day-old cells were loaded with 3 mM fluo-4-acetoxymethyl ester diluted in culture medium, at 37 8C for 30 min Thereafter, the calcium-dye-probe was washed off and exchanged with 2 mL of fresh medium The

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fluorescence emission of the fluo-4-loaded cells, induced by

excitation at 488 nm (laser Ar/Kr) was recorded with a

500-nm long-pass filter on a Noran OZ confocal microscope

(Noran Instruments, Middleton, WI, USA) Images were

recorded as a time series (512  480 pixels at one image per

532 ms) and data processing was carried out using the

INTERVISION software (Noran Instruments) Cyclo128 OP

(1028M) was ejected for 2 s in the vicinity of the cells by a

pressure ejection system

Measurement of cytosolic Ca21concentration

Five- to seven-day-old cells were loaded with 5 mM

indo-1-acetoxymethyl ester diluted in culture medium, at 37 8C

for 45 min The cells were washed twice with 2 mL of fresh

medium The [Ca21]i was monitored by a dual-emission

microfluorimeter system constructed from a Nikon Diaphot

inverted microscope, as previously described [12] The

fluorescence emission of indo-1, induced by excitation at

355 nm, was recorded at two wavelengths (405 nm and

480 nm) by separate photometers (Nikon, Champigny sur

Marne, France) The 405/480 ratio was determined using

an analogic divider (constructed by B Dufy, University of

Bordeaux, France) after conversion of single photon

currents to voltage signals All three signals (405 nm,

480 nm and the 405/480 ratio) were continuously recorded

with the JAD-FLUO 1.2 software (Notocord Systems,

Croissy-sur-Seine, France) The [Ca21]i-values were

calcu-lated as previously described [22] All secretagogues were

ejected for 2 s in the vicinity of individual cells by a pressure

ejection system The indicated doses of peptides correspond

to the concentration contained in the ejection pipette

Measurement of polyphosphoinositide metabolism

Twelve- to 14-day-old cells were incubated with 10 mCi:mL21

myo-[3H]inositol (100 Ci:mmol21) at 37 8C in glucose- and

fetal bovine serum-free culture medium, in the absence or

presence of ODN-related peptides The incubation was

stopped by removing the medium and adding 1 mL of

ice-cold 10% trichloroacetic acid The cells were homogenized

and centrifuged (13 000 g; 15 min; 4 8C) The supernatant

was washed three times with water-saturated diethylether,

neutralized with 10 mL of 1M NaHCO3 Free inositol and

total tritiated inositol phosphates (IPs) were separated by

anion exchange chromatography (AG1-X8 resin; 100 – 200

mesh; formate form; Bio-Rad Laboratories, Richmond, CA,

USA) using distilled water and 0.8Mammonium formate in

0.1M formic acid, respectively, and the radioactivity

contained in each fraction was counted in a b-counter

(LKB 1217 Rack Beta, EG and G Wallace, Evry, France)

Polyphosphoinositides (PIPs) were extracted from the

pellet with 500 mL CHCl3/MeOH (2 : 1, v/v) and counted

in a b-counter The remaining pellets were used for

measurement of protein concentration by the Lowry’s

method

NMR spectroscopy

NMR experiments were carried out using an AVANCE

DMX 600 MHz spectrometer (Bruker S.A., Wissenbourg,

France) equipped with a SGI indigo 2 computer

One-and two-dimensional NMR spectra were obtained at

temperatures of 275, 280, 285, 293 and 298 K NMR samples were prepared by dissolving the peptides in 550 mL

of H2O (10% D2O) or D2O One- and two-dimensional spectra were recorded with carrier frequency in the middle

of the spectrum coinciding with the water resonance which was suppressed either by a presaturation using continuous irradiation during relaxation delay or by using the gradient pulseWATERGATE[23] One- and two-dimensional1H NMR spectra were calibrated using DSS as an external reference Spin systems identification and sequential assignment were achieved by TOCSY, COSY and NOESY experiments The TOCSY spectra were recorded with spin-lock time of 80 ms

by using Mlev17 sequence for the isotropic mixing Four mixing times (80, 150, 200 and 300 ms) were used for NOESY spectra in order to identify diffusion effects All two-dimensional NMR experiments were acquired with

a total of 2048 complex data points in F2, and 512 experiments in F1 Prior to Fourier transform, data matrices were zero filled in F1 dimension and a phase shifted sine-bell filter function was applied Processing of NMR data was performed on a SGI Indigo 2 workstation using the manufacturer’s programs XWINNMR 2.1 and

AURELIA2.0

Structure calculations The volumes of the cross-peaks of the NOESY spectra acquired with a mixing time of 200 ms were integrated using the AURELIA 2.0 software from Bruker Interproton distances were calculated using the isolated spin pair approximation and setting the average methylene cross peak volume at 0.18 nm A range of 20% of the distance values was used for defining the upper and lower bonds of the constraints For the methyl protons and protons that could not be stereospecifically assigned, pseudoatoms were generated during primary structure construction For these protons the lower bond of the distance constraints was set

to the sum of the Van der Waals radii Backbone dihedral restraint residues were deduced from 3JNH-Ha coupling constant by using the empirically Karplus-type relations [24] For coupling constant where more than a single F-value is possible, additional secondary information from NOE data was used to reduce the number of solutions A range of ^ 308 was used for defining the upper and lower angle of the constraints The structures were generated from the experimental data with a standard dynamical simulated annealing protocol using theX-PLOR3.1 program A force field adapted for NMR structure determination (file parallhdg.pro and topallhdg.pro) was used, and an initial structure was built by randomly generating F and C angles

In the calculations starting from random structure, we used higher force constants for the bond lengths, bond angles, improper and planarity angles After a short energy minimization, the first stage started with scaling of the weights of the NOE, constrained improper dihedrals, and nonbonded terms initially small values to more realistic ones using in total 30 000 time steps each of 0.002 ps at 1000 K The second stage performed a slow cooling of the system to

100 K in 50 stages each with 5000 time steps of 0.002 ps The final stage involved 2000 cycles of constrained Powell energy minimization Structures with the lowest distance and dihedral constraint energy were selected and refined by restrained Powell energy minimization using a more

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realistic force field based on theCHARMM19 program The

Van der Waals energy was calculated with switched

Lennard – Jones potential, and the electric energy was

calculated with a shifted Coulomb potential with a dielectric

constant 1 ¼ 80.7 Structures were displayed using the

SYBYLsoftware package (Tripos Associates, Inc., St Louis,

MO, USA) The whole structural analysis described in the

text was performed using structures calculated without

explicit H-bond restraints The final structures were

examined to obtain pairwise root mean square differences

(rmsd) over the backbone heavy atoms (N, Ca and C)

Structure calculations without dihedral constraints were also

carried out This did not produce any structural

modifi-cation, and only a slight change of the rmsd values was

observed for the backbone atoms

Calculations and statistics

Data are expressed as mean ^ SEM Student’s t-test

was used to determine statistical differences between

control and experimental values within the same set of

experiments [25]

R E S U L T S

Synthesis of cyclic peptides

The two cyclic peptides cyclo128OP and cyclo128[D-Leu5]OP

were synthesized directly on solid support and the

head-to-tail cyclization was achieved using orthogonal allyl

protection for the a-carboxylic function of aspartic acid

(Fig 1) After the last coupling cycle and removal of the

allyl protecting group with Pd(0) and N-methylmorpholine,

an aliquot of Fmoc-peptidyl(PEG-PS)-OH was treated with

the cleavage mixture (reagent K) [26] and submitted to

RP-HPLC analysis The chromatograms corresponding to

the different steps of the synthesis of cyclo128OP are shown

in Fig 2 The HPLC profiles revealed the existence of two

peaks which eluted at 17.0 and 26.2 min (Fig 2A) The

major one (retention time 26.2 min), which was assumed to

be the Fmoc-peptidyl-OH derivative, completely vanished

after treatment with piperidine (Fig 2B) After two periods

of 3.5 h of lactamization with intermediate reactivation,

followed by side-chain deprotection and cleavage of the

peptide from the resin, RP-HPLC analysis revealed the occurrence of a new major peak eluting at 18.6 min and the disappearance of the linear precursor form (Fig 2C) Similar chromatograms were obtained during the synthesis

of cyclo128[D-Leu5]OP (data not shown)

Effect of ODN analogs on [Ca21]i The spatial-temporal [Ca21]ichanges in rat astrocytes were visualized by means of a confocal laser scanning microscope Ejection of 1028Mcyclo128OP in the vicinity

of cultured cells provoked a wave of calcium in the cytoplasm of astrocytes (Fig 3A) while ejection of culture medium alone had no effect (Fig 3B) Comparison of the amplitude of the response with that of ODN and OP revealed that, at a concentration of 1028M, cyclo128OP was more efficient than ODN and OP (Fig 3C) Administration of graded concentrations of OP and cyclo128 OP induced a bell-shaped [Ca21]i response (Fig 4) For concentrations ranging from 10211to 1028M, OP and cyclo128OP pro-voked a dose-related increase in [Ca21]i with maximum responses at concentrations of 1028M and 3.16  1029M, respectively At higher concentrations (102721025M), the effect of OP and cyclo128 OP gradually declined The efficacy of cyclo128 OP in raising [Ca21]i was 1.4-fold higher than that of OP Repeated pulses of cyclo128 OP (3.16  1029M) resulted in sequential increases in [Ca21]i with gradual attenuation of the response (Fig 4)

Administration of cyclo128 [D-Leu5]OP, for concentra-tions ranging from 10210to 1025M, did not affect [Ca21]iin rat astrocytes (Fig 5) A 10-min preincubation of astrocytes with graded concentrations of cyclo128 [D-Leu5]OP (1021021026M) provoked a dose-dependent inhibition of the ODN-induced [Ca21]i increase with a pIC50 value of 7.17 ^ 0.29 (Fig 6) At a concentration of 1026M, cyclo128[D-Leu5]OP totally abolished the [Ca21]iresponse

to ODN Cyclo128[D-Leu5]OP also suppressed the [Ca21]i increase evoked by 1028M OP (Fig 7A) On the other hand, cyclo128[D-Leu5]OP, at concentrations of 1026and

1025M, significantly reduced (P , 0.001) but did not abolish the [Ca21]i increase induced by cyclo128 OP (Fig 7B)

Fig 1 Scheme for the stepwise approach in the synthesis of the cyclic peptides (A) (1) piperidine 20% NMP, (2) Fmoc-AA-OH/HBTU/HOBt/ DIEA, (3) Ac 2 O/CHCl 3 /NMM (B) (1) [Ph 3 P] 4 Pd/ AcOH/CHCl 3 /NMM, (2) AcOH/CHCl 3 /NMM, (3) DIEA 0.5% DMF, (4) sodium

diethyldithiocarbamate 0.5% DMF, (5) HOBt 0.5% DMF, (6) DCM; (C) (1) piperidine 20% NMP, (2) HBTU/DIEA; (D) trifluoroacetic acid/ phenol/thioanisol/ethanedithiol/H 2 O Xaa ¼ Leu (cyclo OP) or -Leu (cyclo [ -Leu5]OP).

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Effect of ODN analogs on polyphosphoinositide

metabolism

Exposure of cultured astrocytes to ODN, OP, or cyclo128OP

(1028 each) caused a significant increase in the formation

of [3H]IPs (Fig 8A) and a concomitant decrease in the levels of [3H]PIPs (Fig 8B) In contrast, cyclo128 [D-Leu5]OP, even at a high concentration (1026M), did not affect the basal level of [3H]IPs and [3H]PIPs (Fig 8A,B) In the presence of 1026 M cyclo128 [D-Leu5]OP, the effect of ODN, OP and cyclo128 OP (1028M each) on [3H]IPs and [3H]PIPs was totally abolished (Fig 8C,D) Similarly, incubation of astrocytes

Fig 2 RP-HPLC monitoring of N- and C-terminal deprotections

and on-resin cyclization of the linear precursor of cyclo 128 OP.

Aliquots of the reaction media after allyl ester deprotection (A), Fmoc

removal (B) and cyclization of the linear precursor (C) were cleaved and

injected onto a Vydac C 18 analytical column The dotted lines represent

the profile of the elution gradient (% acetonitrile).

Fig 3 Effect of cyclo 128 OP on [Ca21] i in cultured rat astrocytes Time series of pseudocolor images illustrating [Ca21] i changes in astrocytes loaded with fluo-4-acetoxymethylester (A) Intracellular

Ca21-wave following ejection of cyclo 128 OP (1028M ) (B) Intra-cellular calcium in cells from the same field after ejection of medium alone Sampling rate, 1 image per 532 ms The pseudocolor scale indicates the corresponding [Ca21] i changes expressed in arbitrary units (C) Effects of ODN, OP and cyclo 128 OP (1028M each) on the amplitude of the calcium response measured by microfluorimetry Each value represents the mean amplitude (^ SEM) of the calcium response calculated from at least 10 different dishes from five independent cultures The number of cells studied is indicated in parentheses NS not statistically significant, *P , 0.05, **P , 0.01.

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for 10 min with the phospholipase C inhibitor U73122

(1025M) abrogated the effects of ODN, OP and cyclo128

OP (1028Meach) on [3H]IPs and [3H]PIPs (Fig 8E,F)

NMR solution structure of cyclo128OP

Amino-acid spin systems of cyclo128 OP were readily

identified from two-dimensional COSY and two-dimensional

TOCSY spectra starting from amide protons in the region of

9.5 – 7 p.p.m and were confirmed by inspection of cross-peaks in the high field region corresponding to side-chain through-bond connectivities NOESY data as those pre-sented in Fig 9 were then used to determine the sequential assignments and the chemical shifts reported in Table 1 Amide protons which were relatively slow to exchange with solvent were identified by dissolving cyclo128OP in deuterated solvent D2O Then, one-dimensional 1H-NMR spectra were recorded at regular interval (Fig 10) Due to fast H/D exchange, the amide NH of residues Gly3, Leu5 and Asp6 disappeared rapidly (within one hour or less) compared to the other amide protons

The3JNH-Hacoupling constants for the amide protons of cyclo128OP were measured from the 1D1H-NMR spectrum (Table 1) The 3JNH-Ha coupling constants of the three leucine residues (Leu4, Leu5 and Leu7) differed from the averaged value usually observed for small peptides (< 7 Hz) The examination of short and medium range NOEs (Fig 11), in particular NOE observed between Ha-Pro2 and Ha-Leu4, Ha-Leu5 and NH-Leu7, Ha-Leu6 and NH-Lys8, in combination with the coupling constants and slow H/D exchange of NH-Leu4, NH-Lys8, suggested a first turn centered on the Gly3 and Leu4 residues, and a second one in the region encompassing the Leu5, Asp6 and Leu7 residues In order to better localize the different turns and to identify each type of turn, molecular modeling under experimental NMR restraints was performed

NOEs data and coupling constants detected for cyclo128

OP were used to drive a set of 47 distance and six dihedral angle restraints These restraints were used to generate a set

of 30 structures by simulated annealing as described in Materials and methods All the calculated structures fitted the experimental data quite well and converged with high precision Analysis of the F and C angles showed that all the residues were in the energetically favorable region of the

Fig 5 Effect of graded concentrations of cyclo 128 [ D -Leu5]OP on

[Ca21] i in cultured rat astrocytes A 2-s pulse (arrow) of cyclo 128

[ D -Leu5]OP (1021021025M ) was administered in the vicinity of

different cells The number of cells studied is indicated in parentheses.

Fig 6 Effect of graded concentrations of cyclo 128 [ D -Leu 5 ]OP on the ODN-evoked [Ca21] i increase in cultured rat astrocytes The cells were incubated for 15 min in the absence (W) or presence (X) of cyclo 128 [ D -Leu5]OP (10 210 210 26

M ) before administration of a 2-s pulse of ODN (1028M ) Each value represents the mean amplitude (^ SEM) of the ODN-evoked response calculated from at least four different dishes from two independent cultures The number of cells studied is indicated in parentheses.

Fig 4 Effect of graded concentrations of OP and cyclo 128 OP on

[Ca21] i in cultured rat astrocytes A 2-s pulse of OP (1021121025M )

and cyclo 128 OP (10 211 210 26

M ) was administred in the vicinity of the cells and [Ca 21 ] i was measured by microfluorimetry Each value

represents the mean amplitude (^ SEM) of the calcium response

induced by OP (B) and cyclo 128 OP (X) calculated from at least four

different dishes from two independent cultures The number of cells

studied is indicated in parentheses The inset shows a typical profile of

the calcium response to 2-s pulses of 3.16  1029M cyclo 128 OP

(arrows).

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Ramachandran diagramme Ten structures with the lowest

distance and dihedral constraint energies were selected,

providing a well-defined shape of the backbone foldings of

cyclo128OP (Fig 12) The rmsd value calculated relatively

to the mean structures over all backbone atoms of the cycle

was 0.009 nm

NMR solution structure of cyclo128[D-Leu5]OP

The1H-NMR spectrum of cyclo128[D-Leu5]OP in H2O at

280 K was assigned by using the same strategy as for

cyclo128OP In a first step, two-dimensional spectra COSY

and TOCSY were used for the identification of the

amino-acid spin system In these spectra the glycine residue was

easily identified from its characteristic remote peaks (Ha1,

Ha2) at the amide proton frequency Two glycine-type

remote peaks were clearly observed instead of one expected,

suggesting the existence of two spectroscopically distinct molecular conformers Analysis of other spectra confirmed the occurrence in the solution of two distinct species corresponding to the same primary structure In a second step, sequential assignment was simultaneously conducted for the two conformers by using daN, dbN, and dNN in the NOESY experiments (Fig 13A) At this stage, the origin of the structural heterogeneity was identified as a peptidyl-prolyl cis-trans isomerism of the peptide bond Arg1-Pro2 Some of the spectral data are illustrated in Fig 13B, that show a region of the NOESY spectrum containing the sequential daa(Arg1, Pro2) and dadd0(Arg1, Pro2) connectivities, characteristic of the two isomeric forms The proton chemical shift values of the cis and trans conformers at 280 K are given in Table 2 Amide protons that exchange with solvent were identified by dissolving cyclo128[D-Leu5]OP in D2O Due to fast H/D exchange all

Table 1.1H-NMR assignments,3J HN-Ha coupling constant and backbone angles F, C for cyclo 128 OP at 280 K Chemical shifts are relative to DSS.

Residue

Chemical shift (p.p.m.)

3 J HN-Ha

(Hz)

Backbone angles (8)

Fig 7 Effect of cyclo 128 [ D -Leu5]OP on the

OP- and cyclo 128 OP-evoked [Ca 21 ] i increase

in cultured rat astrocytes The cells were

incubated for 15 min in the absence or presence of

cyclo 128 [ D -Leu5]OP (10 26 or 10 25

M ) before administration of a 2-s pulse (arrow) of OP (A) or

cyclo 128 OP (B) (1028M , each) Each value

represents the mean amplitude (^ SEM) of the

ODN-evoked response calculated from at least 4

different dishes from two independent cultures.

The number of cell studied is indicated in

parentheses.

Trang 8

amide protons of cyclo128[D-Leu5]OP disappeared rapidly

(within one hour or less) (Fig 14)

In the NOESY spectrum, the cross-peaks of the cis and

trans conformers could be clearly separated and analyzed

for structure determination In addition, no exchange of

cross-peak could be observed between the resonances of the

two conformers, indicating that the interconversion is very

slow on the NMR time-scale NOEs detected for trans and

the cis isomers in combination with the coupling constant,

measured from the one-dimensional spectrum, supported

the existence of a well-defined structure and were used to

drive a set of 27 distance and four dihedral angle constraints

for the trans conformer and 31 distance and six dihedral

angle constraints for the cis conformer These restraints

were used to generate a set of 30 structures for each

conformer of cyclo128[D-Leu5]OP using the same protocol

as for cyclo128OP Ten final best structures obtained for the

trans and cis conformers were selected providing a

well-defined shape of the backbone foldings (Fig 15) The rmsd

values calculated relatively to the mean structures over all

backbone atoms of the cycle was 0.009 nm for the trans conformer and 0.007 nm for the cis conformer

D I S C U S S I O N

It has been previously reported that OP is the minimum active sequence of ODN that possesses full agonistic activity

Fig 9 Region of 600- MHz NOESY spectrum of cyclo 128 OP obtained in H 2 O at 280 K The spectrum was recorded with a mixing time of 200 ms.

Fig 8 Effect of cyclo 128 [ D -Leu5]OP and U73122 on inositol

phosphate formation and polyphosphoinositide breakdown induced

by ODN, OP and cyclo 128 OP in cultured rat astrocytes The cells

were incubated for 5 min with ODN, OP or cyclo 128 OP (1028M each)

in the absence (A, B) or presence (C, D) of cyclo 128 [ D -Leu5]OP

(1026 M ) In another set of experiments (E, F), the cells were

preincubated with U73122 (1025M ) for 10 min and then incubated for

5 min with ODN, OP or cyclo 128 OP (10 28

M each) Each bar represents the mean (^ SEM) value from at least three independent

experiments The number of determinations is indicated in parentheses.

**P , 0.01, ***P , 0.001.

Fig 10 Region of 600-MHz amide proton NMR spectra (A) Spectrum of cyclo 128 OP in H 2 O (B – D) Spectra of cyclo 128 OP in

D O recorded after 10, 75 and 255 min, respectively.

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on [Ca21]iin cultured rat astrocytes [12] It has also been shown that the [D-Leu5]OP analog behaves as a weak antagonist in the same in vitro model [12] The present study demonstrates that the cyclic analogs cyclo128 OP and cyclo128[D-Leu5]OP exhibit, respectively, potent agonistic and antagonistic activities both on calcium mobilization and

on polyphosphoinositide metabolism in rat astroglial cells The secondary structure of these two ODN analogs has been determined by combining two-dimensional 1H-NMR and molecular dynamics

Introduction of conformational restraint through cycliza-tion has become a standard strategy in medicinal chemistry for increasing the receptor affinity and selectivity of peptide ligands [13,14,27] The Ala-scan of OP has revealed that the side chain of each residue is required for the full activity

of the peptide [12] These data led us to synthesize cyclic analogs of OP and to use the N- and C-terminus for cyclization in order to keep the side chains unmodified We have taken advantage of the presence of an aspartic acid residue in the core sequence of OP and its analog to carry out

Fig 11 Summary of NOEs observed in a 600-MHz NOESY

spectrum of cyclo 128 OP obtained in H 2 O at 280 K The sequence is

displayed with the one-letter code The heights of the bars indicate the

intensities of the NOEs Residues with exchanging times of amide

protons larger than 1 h are indicated by black squares above the

sequence.

Fig 12 Lowest energy conformer of cyclo 128 OP from simulated

annealing The dotted lines indicate hydrogen bonds consistent with

NMR data.

Fig 14 Summary of NOEs observed in a 600-MHz NOESY spectrum of cyclo 128 [ D -Leu 5 ]OP obtained in H 2 O at 280 K (A) Cis isomer (B) Trans isomer The sequence is displayed with the one-letter code The heights of the bars indicate the intensities of the NOEs.

Fig 13 Regions of a 600-MHz NOESY spectra

of cyclo 128 [ D -Leu5]OP recorded with a mixing

time of 200 ms at 280 K (A) NH-aCH cross

peaks in H 2 O: cis isomer, bold letters; trans

isomer, italic letters (B) aCH-aCH region in D 2 O

solution.

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head-to-tail cyclization on peptides bounded to the resin

according to the strategy of Trzeciak & Bannwarth [19],

rather than cyclization of a protected peptide in solution

With this procedure, aspartic acid was attached to the solid

support via the b-carboxyl group whereas the a-carboxylic

group was protected as allyl ester Monitoring of peptide

deprotection and lactamization processes by analytical

RP-HPLC revealed that the Na-Fmoc group was not totally

stable in reductive media This observation was at variance

with the data reported by Carpino & Han [28], who found

that Fmoc-derivatives are not sensitive to catalytic

hydro-genolysis Such a phenomenon, which has been already

reported by others [29,30], can be ascribed to the occurrence

of traces of dimethylamine in DMF or to the resonance

stabilization properties of the fluorenyl system HPLC

analysis revealed that the peptides were entirely end-to-end

cyclized indicating that the experimental conditions favored

intramolecular rather than intermolecular cyclization The low reticulation grade of the solid support and the PEG spacer used in this study produced a pseudodilution phenomenon [31] and complete solvatation of the reactive sites [32,33] which contributed to the efficacy of the intramolecular cyclization

Using a video imaging confocal microscopy technique,

we found that cyclo128OP induced calcium waves in cultured rat astrocytes, suggesting that cyclization did not impair the agonistic activity of OP Quantitative measurement of [Ca21]i

by microfluorimetry showed that cyclo128OP induced a bell-shaped increase in [Ca21]i which was reminiscent of those previously observed with ODN and OP [12] However, we found that the potency of cyclo128 OP was increased by a factor of three and its efficacy by a factor of 1.4 compared to its linear counterpart in eliciting [Ca21]irise in rat astrocytes

As the dose–response curves obtained with ODN and OP are

Table 2.1H-NMR assignments,3J HN-Ha coupling constant and backbone angles F, C for cis and trans conformers of cyclo 128 [ D -Leu5]OP at

280 K Chemical shift is relative to DSS.

Residue

Chemical shift (p.p.m.)

3

J HN – Ha

(Hz)

Backbone angles (8)

a

Cis conformer.bTrans conformer.

Fig 15 Lowest energy conformers of cyclo 128

[ D -Leu5]OP from simulated annealing (A) Cis conformer (B) Trans conformer.

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