Pseudo-prolines in cyclic peptides: Conformational stabilisation of cyclo[Pro-Thr(Psi(Me,Me)Pro)-Pro]
Ruckle, T; de Lavallaz, P; Keller, M; Dumy, P; Mutter, M
1999

Abstract

Linear peptide H-Pro-Thr(Psi(Me,Me)pro)-Pro-OH containing a preformed cis-Pro-Thr(Psi(Me,Me)pro) tertiary amide bond cyclises instantaneously and free of formation of oligomeric structures to the cyclic tripeptide cyclo-[Pro-Thr(Psi(Me,Me)pro)-Pro]. Even at concentrations up to 10(-1) M peptide, no oligomeric structures are detected by mass spectroscopy and HPLC. 2D H-1 NMR studies of purified cyclotripeptide reveal the compound to exist in one single conformation with all peptide bonds in the cis conformation. These results indicate enhanced cyclisation tendencies of cis-amide bond containing peptides of short chain length. (C) 1999 Elsevier Science Ltd. All rights reserved.

Details

Title Pseudo-prolines in cyclic peptides: Conformational stabilisation of cyclo[Pro-Thr(Psi(Me,Me)Pro)-Pro]
Author(s) Ruckle, T ; de Lavallaz, P ; Keller, M ; Dumy, P ; Mutter, M
Published in Tetrahedron
Volume 55
Issue 37
Pages 11281-11288
Date 1999
ISSN 0040-4020
DOI https://doi.org/10.1016/S0040-4020(99)00650-X
Laboratories LCBP
Record Appears in Scientific production and competences > SB - School of Basic Sciences > SB Archives > LCBP - Laboratory of biomimetic and peptide chemistry
Peer-reviewed publications
Work produced at EPFL
Journal Articles
Published
Record creation date 2006-02-09

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