Abstract | BACKGROUND: PURPOSE: We focused on the cis/trans configurations of the peptide bonds in proline-containing tripeptides in order to discover whether the different structural properties of these peptides influence their activity in ACE-1 inhibition. We hypothesized that the configuration of proline-containing peptides plays a significant role in enzyme inhibition. METHODS: AutoDock 4.2 docking software was used to predict suitable peptide bond configurations of the tripeptides. Besides modeling studies, we completed ACE-1 activity measurements in vitro using HUVEC cultures. RESULTS: In HUVEC cells, both IPP and VPP inhibited ACE-1. Based on molecular docking studies, we propose that in ACE-1 inhibition IPP and VPP share a similar cis configuration between the first aliphatic ( isoleucine or valine) and the second ( proline) amino acid residues and more different configurations between two proline residues. In vivo experiments are needed to validate the significance of the present findings.
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Authors | Aino Siltari, Riikka Viitanen, Sampo Kukkurainen, Heikki Vapaatalo, Jarkko Valjakka |
Journal | Biologics : targets & therapy
(Biologics)
Vol. 8
Pg. 59-65
( 2014)
ISSN: 1177-5475 [Print] New Zealand |
PMID | 24596454
(Publication Type: Journal Article)
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