Chemical properties and application of natural and synthetic polypeptides

• Research unit: COST
• Project number: C96.0037

Key words (English)

PEPTIDE; COIL-COILED; TERTIARY STRUCTURE; CONFORMATION; PROTEIN STRUCTURE; SELF-REPLICATION

Research programs (English)

COST-Action D7 - Molecular recognition chemistry

Short description (English)

See abstract

Partners and International Organizations (English)

B, CH, CZ, D, DK, E, F, FIN, H, I, IRL, N, NL, P, S, SI, UK

Abstract (English)

A 35-peptide was synthesized, which was the pentamer of a heptapeptide having the structure H-Lys-Phe-Glu-Ala-Leu-Glu-Gly-OH The main idea behind the work was to study the association behaviour of the 35-peptide, and in particular to study the coil-coiled interactions. In fact, very similar peptides had been shown in the literature to yield double helices which are capable of self-association. The tertiary structure of this peptide in aqueous solution was investigated by circular dichroic techniques in order to determine the extent of secondary structure (helix) as well as by analytical ultracentrifugation to determine the molecular weight of the aggregates. The results obtained were instrumental in clarifying a series of controversial observations in the literature-among others that the double helices in solution formed trimers and not dimers, as believed until now. An additional aim of the project was to study the possible self-replication of peptides, with the idea of using the 35-peptide as a template. At this regard, only preliminary results could be obtained in this time period.

References in databases (English)

Swiss Database: COST-DB of the State Secretariat for Education and Research Hallwylstrasse 4 CH-3003 Berne, Switzerland Tel. [phone] Swiss Project-Number: C96.0037