Structure-activity relationships of αIIb 313-320 derived peptide inhibitors of human platelet aggregation

Journal of Peptide Science

Volumn 14, Issue 11, 2008, Pages 1195-1202

  Stanica, Ruxandra Maria ^a   Benaki, Dimitra ^b   Rodis, Foteini I ^a   Mikros, Emmanuel ^c   Tsoukatos, Dimokritos ^a   Tselepis, Alexandros ^a   Tsikaris, Vasilios ^a  

^a UNIVERSITY OF IOANNINA   (Greece)

^b INSTITUTE OF NANOSCIENCE AND NANOTECHNOLOGY   (Greece)

^c UNIVERSITY OF ATHENS   (Greece)

Author keywords

IIb binding sites; Arginine interactions; Aspartic acid interactions; Fibrinogen inhibitors; Integrin IIb 3; NMR of peptides; RGD conformations; SARS

Indexed keywords

ALANINE; ALANYLMETHIONYLGLUTAMYLSERYLARGINYLALANYLASPARTYLARGININE; FIBRINOGEN; FIBRINOGEN RECEPTOR; FIBRINOGEN RECEPTOR ANTAGONIST; GLUTAMIC ACID; METHIONINE; OCTAPEPTIDE; PEPTIDE DERIVATIVE; SERINE; SYNTHETIC PEPTIDE; TYROSINE; TYROSYLALANYLGLUTAMYLSERYLARGINYLALANYLASPARTYLARGININE; TYROSYLMETHIONYLALANYLSERYLARGINYLALANYLASPARTYLARGININE; TYROSYLMETHIONYLGLUTAMYLALANYLARGINYLALANYLASPARTYLARGININE; TYROSYLMETHIONYLGLUTAMYLSERYLALANYLALANYLASPARTYLARGININE; TYROSYLMETHIONYLGLUTAMYLSERYLARGINYLALANYLALANYLARGININE; TYROSYLMETHIONYLGLUTAMYLSERYLARGINYLALANYLASPARTYLALANINE; TYROSYLMETHIONYLGLUTAMYLSERYLARGINYLALANYLASPARTYLARGININE; TYROSYLMETHIONYLGLUTAMYLSERYLARGINYLALANYLASPARTYLARGINYLLYSYLLEUCYLALANYLGLUTAMYLVALYLGLYCYLARGINYLVALYLTYROSYLLEUCYLPHENYLALANYLLEUCINE; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ARTICLE; BIOLOGICAL ACTIVITY; CONTROLLED STUDY; DRUG PROTEIN BINDING; HUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PEPTIDE SYNTHESIS; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN FUNCTION; PROTEIN STRUCTURE; SEQUENCE ANALYSIS; SIGNAL TRANSDUCTION; STRUCTURE ACTIVITY RELATION; THROMBOCYTE AGGREGATION INHIBITION;

ARGININE; ASPARTIC ACID; HUMANS; INTEGRIN BETA3; MAGNETIC RESONANCE SPECTROSCOPY; MOLECULAR CONFORMATION; OLIGOPEPTIDES; PEPTIDES; PLATELET AGGREGATION; PLATELET AGGREGATION INHIBITORS; PLATELET MEMBRANE GLYCOPROTEIN IIB; PROTEIN CONFORMATION; SPECTROMETRY, MASS, ELECTROSPRAY IONIZATION; STRUCTURE-ACTIVITY RELATIONSHIP; VON WILLEBRAND FACTOR;

EID: 57849090476     PISSN: 10752617     EISSN: 10991387     Source Type: Journal    
DOI: 10.1002/psc.1060     Document Type: Article

References (34)

1. Philips DR, Charo IF, Parise LV, Fitzgerald LA. The platelet membrane glycoprotein IIb-IIIa complex. Blood 1988; 71: 831-843.
2. Calvete JJ. Platelet integrin GPIIb/IIIa: structure-function correlations. An update and lessons from other integrins. Proc. Soc. Exp. Biol. Med. 1999; 222: 29-38.
3. Giltay JC, Leeksma OC, Breederveld C, van Mourik JA. Normal synthesis and expression of endothelial IIb/IIIa in Glanzmann's thrombasthenia. Blood 1987; 69: 809-812.
4. Tsikaris V. The anti-platelet approach targeting the fibrinogen ligand of the GPIIb/IIIa receptor. J. Pept. Sci. 2004; 10: 589-602.
5. 3. Eur. J. Biochem. 2003; 270: 3760-3767.
6. IIb subunit (Phe289 Ser, Glu324 → Lys and Gln747 → Pro) causing thrombasthenic phenotypes in four Japanese patients. Br. J. Haematol. 1998; 102: 829-840.
7. Ferrer M, Fernandez-Pinel M, Gonzalez-Manchon C, Gonzalez J, Ayuso MS, Parrilla R. A mutant (Arg327 → His) GPIIb associated to thrombasthenia exerts a dominant negative effect in stably transfected CHO cells. Thromb. Haemostasis 1996; 76: 292-301.
8. Ruan J, Peyruchaud O, Alberio L, Valles G, Clemetson K, Bourre F, Nurden AT. Double heterozygosity of the GPIIb gene in a Swiss patient with Glanzmann's thrombasthenia. Br. J. Haematol. 1998; 102: 918-925.
9. Tao J, Arias-Sagado EG, Gonzalez-Manchon C, Iruin G, Butta N, Ayuso MS, Parrilla R. A 1063G → A mutation in exon 12 of glycoprotein (GP) IIb associated with a thrombasthenic phenotype: mutation analysis of [324E] GPIIb. Br. J. Haematol. 2000; 111: 965-973.
10. 3. Biochem. J. 1997; 325: 309-313.
11. 3 on resting platelets and causes resting platelet aggregate formation without platelet shape change. Thromb. Res. 1998; 89: 31-40.
12. 3 interacting peptide. Thromb. Haemostasis 2001; 86: 894-901.
13. 3. Eur. J. Biochem. 2004; 271: 855-862.
14. 3. Platelets 2006; 17: 277-282.
15. Jones J. Abbreviations and symbols in peptide science: a revised guide and commentary. J. Pept. Sci. 2006; 12: 1-12.
16. Stewart JM, Young JD. Solid Phase Peptide Synthesis. Pierce Chem. Co.: Rockford, IL, 1984; 71-95.
17. Atherton E, Sheppard RC. Solid Phase Peptide Synthesis: A Practical Approach. IRL Press: Oxford, 1989.
18. Bodansky M, Bodansky A. The Practice of Peptide Synthesis, 2nd edn. Springer: Berlin, 1994.
19. 1H NMR studies on the preferred interactions of guanidinium and C-terminal carboxylate groups in arginine containing peptides. J. Chem. Soc., Perkin Trans. 2 1993; 1345-1349.
20. Bax A, Davis DG. MLEV-17-based two-dimensional homonuclear magnetization transfer spectroscopy. J. Magn. Reson. 1985; 65: 355-360.
21. Kumar A, Ernst RR, Wüthrich K. A two-dimensional nuclear Overhauser enhancement (2D NOE) experiment for the elucidation of complete proton-proton cross-relaxation networks in biological macromolecules. Biochem. Biophys. Res. Commun. 1980; 95: 1-6.
22. Brunger AT, Adams PD, Clore GM, DeLano WL, Gros P, Grosse-Kunstleve RW, Jiang JS, Kuszewski J, Nilges M, Pannu NS, Read RJ, Rice LM, Simonson T, Warren GL. Crystallography and NMR system. A new software suite for macromolecular structure determination. Acta Crystallogr., Sect. D 1998; 54: 905-921.
23. Shenkin PS, McDonald DQ. Cluster-analysis of molecular conformations. J. Comput. Chem. 1994; 15: 899-916.
24. Mohamadi F, Richards NGJ, Guida WC, Liskamp R, Lipton M, Caufield C, Chang G, Hendrickson T, Still WC. MACROMODEL. An integrated software system for modeling organic and bioorganic molecules using molecular mechanics. J. Comput. Chem. 1990; 11: 440-467.
25. 2 peptide as a probe of slow conformational exchange of short linear peptides in DMSO. Biopolymers 2003; 69: 72-86.
26. n) for multiple anchoring of antigenic peptides: application to the acetylcholine receptor (AChR) main immunogenic region. Int. J. Biol. Macromol. 1996; 19: 195-205.
27. 1H NMR studies on arginine tripeptides: evidence for guanidinium-C-terminal carboxylate interactions. Pept. Res. 1992; 5: 110-114.
28. Tsikaris V, Sakarellos-Daitsiotis M, Tzovaras D, Sakarellos C, Orlewski P, Cung MT, Marraud M. Isomerization of the Xaa-Pro peptide bond induced by ionic interactions of arginine. Biopolymers 1996; 38: 673-682.
29. Tsikaris V, Cung MT, Sakarellos C, Tzinia AK, Soteriadou KP, Sakarellos-Daitsiotis M. NMR study on a SRYD-containing fibronectin-like sequence (250-257) of Leismania gp63: Contribution of residual water in the dimethyl sulfoxide solution structure. J. Chem. Soc., Perkin Trans. 2 1994; 821-826.
30. Kostidis S, Stavrakoudis A, Biris N, Tsoukatos D, Sakarellos C, Tsikaris V. The relative orientation of the Arg and Asp side chains defined by a pseudodihedral angle as a key criterion for evaluating the structure-activity relationship of RGD peptides. J. Pept. Sci. 2004; 8: 494-509.
31. Benedetti E, Morelli G, Némethy G, Scheraga HA. Statistical and energetic analysis of side-chain conformations in oligopeptides. Int. J. Pept. Protein Res. 1983; 22: 1-15.
32. McGregor MJ, Islam SA, Sternberg MJ. Analysis of the relationship between side-chain conformation and secondary structure in globular proteins. J. Mol. Biol. 1987; 198: 295-310.
33. Stavrakoudis A, Bizos G, Eleftheriadis D, Kouki A, Panou-Pomonis E, Sakarellos-Daitsiotis M, Sakarellos C, Tsoukatos D, Tsikaris V. A three-residue cyclic scaffold of non-RGD containing peptide analogues as platelet aggregation inhibitors: design, synthesis, and structure-function relationships. Biopolymers 2001; 56: 20-26.
34. Kouki A, Mitsios JV, Sakarellos-Daitsiotis M, Sakarellos C, Tselepis AD, Tsikaris V, Tsoukatos DC. Highly constrained cyclic (S,S)-CXaaC-peptides as inhibitors of fibrinogen binding to platelets. J. Thromb. Haemostasis 2005; 3: 2324-2330.