Circular dichroism and Fourier transform infrared spectroscopic studies on self-assembly of tetrapeptide derivative in solution and solvated film

Journal of Peptide Research

Volumn 61, Issue 3, 2003, Pages 122-128

  Ganesh, S ^a   Jayakumar, R ^a  

^a CENTRAL LEATHER RESEARCH INSTITUTE   (India)

Author keywords

Beta sheet; Conformational transition; Helical turn; Peptide assemblage; Tetramer; Tetrapeptide

Indexed keywords

METHANOL; TETRAPEPTIDE;

ARTICLE; BINDING SITE; CIRCULAR DICHROISM; FILM; FLUORESCENCE SPECTROSCOPY; FOURIER TRANSFORMATION; INFRARED SPECTROSCOPY; PEPTIDE ANALYSIS; PRIORITY JOURNAL; PROTON NUCLEAR MAGNETIC RESONANCE;

CIRCULAR DICHROISM; DOSE-RESPONSE RELATIONSHIP, DRUG; METHANOL; PEPTIDES; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; SPECTROMETRY, FLUORESCENCE; SPECTROSCOPY, FOURIER TRANSFORM INFRARED;

EID: 0037371757     PISSN: 1397002X     EISSN: None     Source Type: Journal    
DOI: 10.1034/j.1399-3011.2003.00039.x     Document Type: Article

References (53)

1. Iqbal, M. & Balaram, P. (1981) Membrane channel forming polypeptides, 270-MHz proton magnetic resonance studies of the aggregation of the 11-21 fragment of suzukacillin in organic solvents. Biochemistry 20, 7278-7284.
2. Raj, P.A. & Balaram, P. (1985) Conformational effects on peptide aggregation in organic solvents: spectroscopic studies of two chemotactic tripeptide analogs. Biopolymers 24, 1131-1146.
3. Ray, A. (1971) Solvophobic interactions and micelle formation in structure forming nonaqueous solvents. Nature 231, 313-315.
4. Friberg, S.E. & Liang, Y.C. (1987) Critical phenomena in nonaqueous micromolecules. Colloid Surf. 24, 325-336.
5. 2H] hexadecyltriethylammonium bromide in micellar solution of nonaqueous polar solvents and their mixtures with water. Langmuir 6, 1205-1211.
6. Ramadan, M., Evana, D.F., Lumry, R. & Phillion, S. (1985) Micelle formation in hydrazine-water mixture. J. Phys. Chem. 89, 3405-3408.
7. Evans, D.F., Yamauchi, A., Wei, G.J. & Bloomfield, V.A. (1983) Micelle size in ethylammonium nitrate as determined by classical and quari-elastic light scattering. J. Phys. Chem. 87, 3537-3541.
8. Guo, H. & Karplus, M. (1994) Solvent influence on the stability of the peptide hydrogen bond: a supramolecular effect. J. Phys Chem. 98, 7104-7105.
9. Ghadiri, M.R., Granja, J.R, Milligan, R.A., McRee, D.E. & Khazanovich, N. (1993) Self-assembling organic nanotubes based on a cyclic peptide architecture. Nature 366, 324-327.
10. Zhang, S., Holmes, T., Lockshin, C. & Rich, A. (1993) Spontaneous assembly of a self-complementary oligopeptide to form a stable macroscopic membrane. Proc. Natl Acad. Sci. USA 90, 3334-3338.
11. Jayakumar, R., Jeevan, R.G., Mandal, A.B. & Manoharan, P.T. (1994) Aggregation, hydrogen bonding and thermodynamic studies on Boc-Val-Val-Val-OMe tripeptide micelles in chloroform. J. Chem. Soc., Faraday Trans. 90, 2725-2730.
12. Jayakumar, R., Mandal, A.B. & Manoharan, P.T. (1993) Micelle formation of Boc-Val-Val-Ile-OMe tripeptide in chloroform and its conformational analysis. J. Chem. Soc., Chem. Commun. 853-855.
13. Jayakumar, R., Jayanthi, C. & Gomathy, L. (1995) Peptide aggregates: a novel model system to study self-assembly of peptides. Int. J. Peptide Protein. Res. 45, 129-137.
14. Mandal, A.B. & Jayakumar, R. (1993) A new micelle-forming peptide. J. Chem. Soc., Chem. Commun. 237-238.
15. Murugesan, M., Jayakumar, R. & Durai, V. (1996) Self-assembly of a nonionic peptide surfactant in aqueous medium. Langmuir 12, 1760-1764.
16. 2 dipeptide. Part 1. Physico-chemical studies on the micelle formation of a dipeptide in the absence and presence of ionic surfactants. J. Chem. Soc., Faraday Trans. 89, 3075-3079.
17. Menger, F.M., Yamasaki, Y., Catlin, K.K. & Nishimi, T. (1995) X-Ray structure of a self-assembled gelating fiber. Angew. Chem., Int. Ed. Engl. 34, 585-586.
18. 5-OMe in chloroform and N,N-dimethylformamaide. Langmuir 16, 1489-1496.
19. Stock, H.T., Turner, N.J. & MeCague, R. [1995) N-(2-Carbonylbenzoyl)-Lphenylalanylglycine: a low molecular-mass gelling agent. J. Chem. Soc., Chem. Commun. 2063-2064.
20. De Loos, M., Van Esch, J.H., Stokroos, I., Kellog, R.M. & Feringa, B.L. (1997) Remarkable stabilization of self-assembled organogels by polymerization. J. Am. Chem. Soc. 119, 12675.
21. Fuhrhop, J.H., Schnieder, P., Boekema, E. & Helfrich, W. (1988) Lipid bilayer fibers from diastereomeric and enentiomeric N-octylaldonamides. J. Am. Chem. Soc. 110, 2861-2867.
22. Burdick, D., Soreghan, B., Kwon, M., Kosmoski, J., Knaue, M., Henschen, A., Yates, J., Cotman, C. & Glabe, C. (1992) Assemblage and aggregation properties of synthetic Alzheimer's A4/β amyloid peptide analogs. J. Biol. Chem. 267, 546-554.
23. Halverson, K., Fraser, P.E., Kirschner, D.A. & Lansbury, J.P. (1990) Molecular determinants of amyloid deposition in Alzheimer's disease: conformational studies of synthetic β-protein fragments. Biochemistry 29, 2639-2644.
24. 4 peptides of Alzheimer's disease. J. Mol. Biol. 218, 149-163.
25. El-Agnaf, O.M., Bodles, A.M., Guthrie, D.J., Harriott, P. & Irvine, G.B. (1998) The N-terminal region of non-A beta component of Alzheimer's disease amyloid is responsible for its tendency to assume beta-sheet and aggregate to form fibrils. Eur. J. Biochem. 258, 157-163.
26. Chiti, F., Webster, P., Tanddei, N., Chark, A., Stefani, M., Ramponi, G. & Dobson, C.M. (1999) Designing conditions for in vitro formation of amyloid protofilaments and fibrils. Proc. Natl Acad. Sci. USA 96, 3590-3594.
27. Walsh, D.M., Hartley, D.M., Kusumoto, Y., Fezoni, Y., Condron, M.M., Lomakin, A., Benedek, G.B., Selkol, D.T. & Teplour, D.B. (1999) Amyloid beta-protein fibrillogenesis. Structure and biological activity of protofibrillar intermediates. J. Biol. Chem. 274, 25945-25952.
28. Weisreb, P.H, Zhenw Poon, A.W., Conway, K.A. & Lansbury, P.T. (1996) NACP, a protein implicated in Alzheimer's disease and learning, is natively unfolded. Biochemistry 35, 13709-13715.
29. Rochet, J.C. & Lansbury, P.T. (2000) Amyloid fibrillogenesis: themes and variations. Curr. Opin. Struct Biol. 10, 60-68.
30. Gasset, M., Baldwin, M.A., Liod, D.H., Mutter, J.M., Holtzman, D.M., Choen, F., Fletterick, R. & Prusiner, S.B. (1992) Predicted alpha-helical regions of the prion protein when synthesized as peptides form amyloid. Proc. Natl Acad. Sci. USA 89, 10940-10944.
31. Blondelle, S.E., Forood, B., Houghten, R.A. & Perez-Paya, E. (1997) Polyalanine-based peptides as models for self-associated β-pleated-sheet complexes. Biochemistry 36, 8393-8400.
32. Ganesh, S. & Jayakumar, R. (2002) The role of N-t-Boc group in helix initiation in a novel tetrapeptide. J. Peptide Res. 59, 249-256.
33. Pike, J., Walencewicz-Wasserman, J., Kosmoski, J., Cribbs, D.H., Glabe, C.G. & Cotman, C.W. (1995) Structure-activity analyses of β-amyloid peptides: contributions of the β25-35 region to aggregation and neurotoxicity. J. Neurochem. 64, 253-265.
34. El-Agnaf, O.M., Brent Irvine, G., Fitzpatrick, G., Kenneth Glass, W. & Guthrie, J.S. (1998) Comparative studies on peptides representing the so-called tachykinin-like region of the Alzheimer Abeta peptide [Abeta (25-35)]. Biochem J. 336, 419-427.
35. Lansbury, P.T. Jr (1999) Evolution of amyloid: what normal protein folding may tell us about fibrillogenesis and disease. Proc. Natl Acad. Sci USA 96, 3342-3344.
36. Herzfeld, J. (1996) Entropically driven order in crowded solutions: from liquid crystals to cell biology. Acc. Chem. Res. 29, 31-37.
37. Slavik, J. (1982) Anilinonaphthalene sulfonate as a probe of membrane composition and function. Biochem. Biophys. Acta 694, 1-25.
38. Murugesan, M., Venugopal, M. & Jayakumar, R. (1997) Aggregation of a tertrapeptide derivative [Boc-Ile. Gly-Met-Thr(Bzl)-Obzl] in chloroform. J. Chem. Soc., Perkin Trans. 2, 1959-1963.
39. Iftime, G., Labarthet, F.L., Natansohn, A. & Rochon, P. (2000) Control of chirality of an azobenzene liquid crystalline polymer with circularly polarized light. J. Am. Chem. Soc. 122, 12646-12650.
40. Taylor, K.S., Lou, M.Z., Chin, T.M., Yang, N.C. & Garavito, R.M. (1996) A novel, multilayer structure of a helical peptide. Protein Sci. 5, 414-421.
41. 4-(1-40)-peptide of Alzheimer's disease. Eur. J. Biochem. 233, 293-298.
42. Toniolo, C., Bonora, G.M., Salardi, S. & Mutter, M. (1979) Linear oligopeptides. A circular dichroism study of α-helix and β-structure formation in solution by homooligo-L-methionines. Macromolecules 12, 620-625.
43. Fasman, G.D. & Potter, J. (1967) The optical rotatory dispersion of two beta structures. Biochem. Biophys Res. Commun 27, 209-216.
44. Widmer, U., Lorenzi, G.P. & Pino, P. (1979) The Influence of Asymmetric Carbon atoms of the side chains on the conformational properties of polypeptides: Comparison of Diastereomeric Homooligopeptides of L-Isoleucine and D-Alloisoleucine. Biopolymers. 18, 239-256.
45. Hu, H.Y., Li, Q., Du Cheng, H.C., Valle, G., Crisma, M., Moretto, V., Isdebski, J., Pelka, J. & Schneider, C.H. (1990) β-Sheet Structure Formation of Proteins in Solid State as Revealed by Circular Dichroism Spectroscopy. Biopolymers 62, 15-21.
46. Toniolo, C., Valle, G., Crisma, M., Moretto, V., Isdebski, & Schneider, C.H. (1990) N-Acylureas in Peptide Synthesis: An X-ray Diffraction and IR-Absorption Study. Helv. Chim. Acta. 73, 626.
47. 6. Bioorg. Med. Chem. Lett 3, 153-156.
48. Zhong, Q., Clark. Lewis, I. & Cushley, R. (1994) Secondary structures of lipid-associating peptides: a Fourier transform infrared study. J. Peptide Res. 7, 99-106.
49. Donaldson, L.W., Petersen, J.M., Graves, B.J. & McIntosh, L.P. (1994) Secondary Structure of the ETS domains places murine Ets-1 in the superfamily of winged helix-turn-helix DNA-binding proteins. Biochemistry 33, 13509.
50. Blondelle, S.E., Forood, B., Houghten, R.A. & Perez-Paya, E. (1997) Polyalanine-based peptides as models for self-associated beta-pleated-sheet complexes. Biochemistry 36, 8393-8400.
51. Bodanszky, M. & Bodanszky, A. (1984) The Practice of Peptide Synthesis Vol.21.
52. Hirsch, W. & Timasheff, S.N., eds (1977) The Synthesis of Peptides by Homogeneous Solution Procedures. Methods in Enzymology XLVII, 512-517.
53. Safer, J., Roller, P.P., Ruben, G.C., Gajdusek, D.C. & Gibbs, C.J. (1993) Secondary structure of proteins associated in thin films. Biopolymers 33, 1461-1476.