CD investigations on conformation of H-X-[Pro]n-Y-OH peptides [X-Trp, Tyr; Y-Tyr, Met]; models for intramolecular long range electron transfer

• Autorzy: Wierzchowski K. L. , Majcher K. , Poznanski J.
• Języki publikacji: EN

Abstrakty

EN

Conformations of three series of peptides: H-Trp-(Pro)n-Tyr-OH (n = 1-5), H-Trp-(Pro)n-Met-OH (n = 1-3) and H-Tyr-(Pro)n-Met-OH (n = 1-3), used as models in studies on long range electron transfer through protein matrix, were investigated by CD spectroscopy in aqueous solution at pH 5.2 in the temperature range of 10°C-90°C. CD spectra of their component N- and C-terminal dipeptide and oligoproline fragments were also measured under similar conditions. In interpretation of the spectra the cis <-> trans equilibrium about X-Pro bonds was taken into account and CD spectra of Trp-Pro and Tyr-Pro chromophores in trans and cis configuration of the peptide bond were evaluated. The spectra of n = 3-5 peptides from the first series and those with n = 2-3 from the other two series exhibit a strong negative band in the 202-207 nm region, the strength of which is proportional to the number of Pro residues in the (Pro)n bridge, and characterized by a large temperature decrement. In view of close similarity between characteristics of this band and the 206 nm band of aqueous oligoproline peptides = 3), known to attain a left handed helical conformation similar to that of 31 helix of the all-trans poly-L-proline II, this band was attributed to a conformation of the latter type. H-Trp-(Pro)2-Tyr-OH does not form this conformation due to sterical interaction between the two bulky aromatic side chains. Conclusions drawn from analysis of the CD spectra are supported by 1H and C13 NMR data reported elsewhere (Poznański et al., 1993, Biopolymers 33,781-795).

Słowa kluczowe

EN

conformation; protein matrix; peptide; circular dichroism; oligoproline peptide

• Wydawca: -
• Czasopismo: Acta Biochimica Polonica
• Rocznik: 1995
• Tom: 42
• Numer: 2
• Opis fizyczny: p.259-268,fig.

Twórcy

autor

Wierzchowski K. L.

• Polish Academy of Sciences, A.Pawinskiego 5a, 02-106 Warsaw, Poland

autor

Majcher K.

autor

Poznanski J.

Bibliografia

• 1. Bobrowski, K., Wierzchowski, K.L., Hoicman, J. & Ciurak, M. (1987) Intramolecular charge transfer between tryptophan and tyrosine in peptides with bridging prolines. Studia biophysica 122,23-28.
• 2. Bobrowski, K., Wierzchowski, K.L., Hoicman, J. & Ciurak, M. (1990) Intramolecular electron transfer in peptides containing methionine, tryptophan and tyrosine: a pulse radiolysis study. Int.}. Radiat. Biol 57,919-932.
• 3. DeFelippis, M.R,, Faraggi, M. & Klapper, M.H. (1990) Evidence for through-bond long-range electron transfer in peptides. J. Am. Chem. Soc. 112,5640-5642.
• 4. Faraggi, M., DeFelippis, M.R. & Klapper, M.H. (1989) Long-range electron transfer between tyrosine and tryptophan in peptides. J. Am. Chem. Soc. Ill, 5141-5145.
• 5. Faraggi, M. & Klapper, M.H. (1990) Intra­molecular electron transfer reactions in peptides and proteins; in Excess Electrons in Dielectric Media (Ferradini, C., Jay-Cerin, J.-R, eds.) pp. 397-423, CRC Press, Boca Raton.
• 6. Bobrowski, K., Hoicman, J., Poznanski, J., Ciurak, M. & Wierzchowski, K.L. (1992) Pulse radiolysis studies of intramolecular electron transfer in model peptides and proteins. 5. Trp'->Tyr' radical transformation in H-Trp- -(Pro)n-Tyr-OH series of peptides. J. Phys. Chem. 96,10036-10043.
• 7. Mishra, A.K., Chandrasekar, R., Faraggi, M. & Klapper, M.H. (1994) Long-range electron transfer in peptides. Tyrosine reduction of the indolyl radical: reaction mechanism, modulation of reaction rate, and physiological considerations./. Am. Chem. Soc. 116,1414-1422.
• 8. Bobrowski, K., Wierzchowski, K.L., Hoicman, J. & Ciurak, M. (1992) Pulse radiolysis studies of intramolecular electron transfer in model peptides and proteins. IV. Met/S.'.Br —> Tyr/O' radical transformation in aqueous solution of H-Tyr-(Pro)n-Met-OH peptides. Int. J. Radiat. Biol. 62,507-516.
• 9. Poznanski, J., Ejchart, A., Wierzchowski, K.L. & Ciurak, M. (1993) *H- and 13C-NMR investi­gations on cis-trans isomerization of proline peptide bonds and conformation of aromatic side chains in H-Trp-(Pro)n-Tyr-OH peptides. Biopolymers 33,781-795.
• 10. Poznanski, J. (1995) Modelowanie wewnątrz- cząsteczkowego przeniesienia elektronu w peptydach zawierających tryptofan i tyrozynę. Ph.D. Dissertation (Institute of Biochemistry and Biophysics, Polish Academy of Sciences, Warszawa) (in Polish).
• 11. Ramachandran, G.N. & Sasisekharan, V. (1968) Conformation of polypeptides and proteins. Adv. Protein Chem. 23,283-437.
• 12. Helbecque, N. & Loucheux-Lefebvre, M.H. (1982) Critical chain length for polyproline-II structure formation in H-Gly-(Pro)n-OH. Int. /. Peptide Protein Res. 19, 94-101.
• 13. Dukor, R.K. & Keiderling, T.A. (1991) Reassessment of the random coil conformation: vibrational CD study of proline oligopeptides and related polypeptides. Biopolymers 31, 1747-1761.
• 14. Rabanal, F., Ludevit, M.D., Pons, M. & Giralt, E. (1993) CD of proline-rich polypeptides: application to the study of the repetitive domain of maize glutelin-2. Biopolymers 33,1019-1028.
• 15. Okabayashi, H., Isemura, T. & Sakakibara, S. (1968) Steric structure of L-proline oligopeptides. II. Far-ultraviolet absorption spectra and optical rotations of L-proline oligopeptides. Biopolymers 6,323-330.
• 16. Ganser, V., Engel, J., Winklmair, D. & Krause, G. (1970) Cooperative transition between two helical conformations in a linear system: poly-L-proline I II. I. Equilibrium studies. Biopolymers 9,329-352.
• 17. Woody, R.W. (1977) Optical rotatory properties of biopolymers. J. Polymer Sei.: Macromolecular Rev. 12,181-321.
• 18. Rothe, M., Rott, H. & Mazanek, J. (1976) Solid state synthesis and conformation of monodisperse high molecular weight oligo-L-proIines; in Peptides 1976 (Loffet, A., ed.) pp. 309-318, Editions de l'Université de Bruxelles, Bruxelles.
• 19. Ronish, E.W. & Krimm, S. (1974) The calculated circular dichroism of polyproline II in the polarizabiiity approximation. Biopolymers 13, 1635-1651.
• 20. Woody, R.W. (1985) Circular dichroism of peptides; in The Peptides: Analysis, Synthesis, Biology (Treatise Editors: Udenfriend, S. & Meienhoffer, J.) Conformation in Biology and Drug Design (Hruby, V.J., ed.) vol. 7, pp. 15-114, Academic Press, New York.
• 21. Edelhoch, H. (1967) Spectroscopic determina­tion of tryptophan and tyrosine in proteins. Biochemistry 6,1948-1954.22. Auer, H.E. (1973) Far ultraviolet absorption and circular dichroism spectra of L-tryptophan and some derivatives. J. Am. Chem. Soc. 95, 3003-3011.
• 23. Matsuura, H., Hasegawa, K. & Miyazawa, T. (1982) Circular dichroism of N-acetyl-L-amino acid methylamides with aromatic side groups. Bull. Chem. Soc. Jpn. 55,1999-2004.
• 22. Goux, W.J. & Hooker, T.M., Jr. (1980) Chiroptical properties of proteins. 1. Near-ultraviolet circular dichroism of ribonuclease S. }. Am. Chem. Soc. 102, 7080-7087.
• 23. Manning, M.C. & Woody, R.W. (1991) Theoretical CD studies of polypeptide helices: examination of important electronic and geometric factors. Biopolymers 31,569-586.
• 24. Thomasson, K.A. & Applequist, J. (1991) Effects of proline ring conformation on theoretical tc-ti* absorption and CD spectra of helical poly(L-proline) forms I and II. Biopolymers 31, 529-535.
• 25. Loomis, R.E., Gonzales, M. & Loomis, P.M. (1991) Investigation of cisjtrans proline isomerism in a multiply occurring peptide fragment from human salivary proline-rich glycoprotein. Int. ). Peptide Protein Res. 38, 428-439.
• 26. Thomas, L.M., Ramasubbu, N. & Bhandary K.K. (1994) Structural characteristics of diproline: a new crystal form of tBoc- -Pro-Pro-OH. Int. f. Peptide Protein Res. 44, 207-214.
• 27. MacArthur, M.W. & Thornton, J.M. (1991) Influence of proline residues on protein conformation. J. Mol Biol. 218, 397-412.