Collect. Czech. Chem. Commun. 2003, 68, 1309-1318

Circular Dichroism and Conformation of Oostatic Peptides: The Carrier-Like Role of C-Terminal Oligoproline Sequence

Petr Maloňa,*, Helena Dlouháa, Blanka Bennettováb, Richard Tykvaa and Jan Hlaváčeka

a Institute of Organic Chemistry and Biochemistry, Academy of Sciences of the Czech Republic, 166 10 Prague 6, Czech Republic
b Institute of Entomology, Academy of Sciences of the Czech Republic, 370 05 České Budějovice, Czech Republic


Circular dichroism spectra of the peptides H-Tyr-Asp-Pro-OH, H-Tyr-Asp-Pro-Ala-OH, H-Tyr-Asp-Pro-Ala-(Pro)n-OH (n = 1-6) and of their two methyleneoxy isosters were measured and analyzed in terms of possible interactions between the N-terminal (mostly tetrapeptide) part that is responsible for the oostatic activity and the C-terminal oligoproline sequence. The results indicate that the two parts are largely independent and that the C-terminal (Pro)n sequence serves another purpose, possibly as a carrier.

Keywords: Peptides; Hormones; Oostatic factors; Proline; CD spectroscopy; Conformation analysis.

References: 16 live references.