theoretical conformational analysis of chemotactic peptides formyl-met-leu-phe-ome and formyl-met-acc6-phe-ome
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ID: 146700
2001
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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.
| Reference Key |
ezzamarty2001internationaltheoretical
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|---|---|
| Authors | ;Aziz Ezzamarty;Mahjoub Lakhdar;Chakib Ameziane Hassani;Youssef Wazady |
| Journal | Intertax |
| Year | 2001 |
| DOI |
10.3390/i2010001
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| URL | |
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