ISSN:
0006-3525
Keywords:
Chemistry
;
Polymer and Materials Science
Source:
Wiley InterScience Backfile Collection 1832-2000
Topics:
Chemistry and Pharmacology
Notes:
The molecular and crystal structures of three monothiated analogues of the blocked L-Ala-Aib-L-Ala sequence of peptaibol antibiotics, t-Boc-L-Ala-Aib-ψ(CSNH)-L-Ala-OMe, Ac-L-Ala-Aib-ψ(CSNH)-L-Ala-OMe, and Ac-ψ(CSNH)-L-Ala-Aib-L-Ala-OMe, determined by x-ray diffraction analyses, are reported. In all cases the peptide chain is folded with ϕ,ψ angles close to or slightly distorted from those expected for a type II β-bend conformation. However, the 4 → 1 H-bond distance falls within the accepted limits only for Ac-L-Ala-Aib-ψ(CSNH)-L-Ala-OMe. The structures are compared with those already published for their two oxygenated analogues.
Additional Material:
6 Ill.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1002/bip.360270504