Abstract:
:Bis-cystine cyclic peptides are a new kind of molecules with potential use as cavitands, transporters or antagonists of target ligands. Studies aimed at establishing their conformational profiles may prove useful in understanding their characteristics and potentiate their use in molecular design. The present investigation reports the results of a computational study devoted to establishing the conformational preferences of model bis-cystine cyclic peptides and the properties in common with their linear analogs. For this purpose a study of four model compounds: (Ac-Cys-X-Cys-NHMe)2 and (Ac-Cys-X-X-Cys-NHMe)2 with X = Ala, Val, was performed. The goal of the study was to explore the importance of the conformational nature of the central residues, the effect of the number of them, and the loss of conformational freedom after cyclization on model molecules. Accordingly, the conformational space and the dynamic behaviour of the four cyclic peptides as well as the corresponding linear analogs was carefully explored. The results indicate the existence of structural patterns that might be useful for the use of this kind of molecule in de novo molecular design.
journal_name
Int J Biol Macromoljournal_title
International journal of biological macromoleculesauthors
Fernandez Y,Ricart JM,Perez JJdoi
10.1016/0141-8130(95)01083-1subject
Has Abstractpub_date
1996-06-01 00:00:00pages
263-74issue
4eissn
0141-8130issn
1879-0003pii
0141813095010831journal_volume
18pub_type
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