Abstract
In order to investigate the proper peptide backbone conformation that is biologically active, the chemotactic peptides formyl-Met-Leu-Phe-OMe and formyl-Met-Acc6-Phe-OMe (Acc6 is the a-a disubstituted amino acid l-aminocyclohexane-1-carboxylic acid) were studied by the theoretical method PEPSEA. This study shows that the parent peptide formyl-Met-Leu-Phe-OMe has a flexible structure, and that the other conformationally constrained peptide has a tendency to form the b turn structure. It also gives evidence against the hypothesis proposing the importance of a formyl group in the interaction with the receptor.
Highlights
Considerable interest has been focused on the chemotactic peptide formyl-Met-LeuPhe-OH "fMLPOH" which has been shown to induce lysosomal enzyme release, thereby playing a very important role in the immunological system
The main objective of this study is to find the active conformation of chemotactic peptides
We find the relative free energy ∆G calculated for T = 300 K, and the relative conformational energy ∆E
Summary
Considerable interest has been focused on the chemotactic peptide formyl-Met-LeuPhe-OH "fMLPOH" which has been shown to induce lysosomal enzyme release, thereby playing a very important role in the immunological system. Since it was reputed to be a very active agent [1], various. 2001, 2 studies have been realized in order to better understand this tripeptide. The influence of terminal groups has been studied, and it has been demonstrated that the esterification of the C-terminal carboxylic acid group does not result in loss of biological activity of molecule [2]. The replacement of the N-terminal formyl group by tert-butyloxycarbonyl group (Boc) induces a dramatic loss of activity [3]
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