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Temporin A and its retro‐analogues: synthesis, conformational analysis and antimicrobial activities
Author(s) -
Kamysz Wojciech,
Mickiewicz Beata,
RodziewiczMotowidło Sylwia,
Greber Katarzyna,
Okrój Marcin
Publication year - 2006
Publication title -
journal of peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 66
eISSN - 1099-1387
pISSN - 1075-2617
DOI - 10.1002/psc.762
Subject(s) - antimicrobial , chemistry , combinatorial chemistry , stereochemistry , computational biology , nanotechnology , biology , materials science , organic chemistry
Temporin A (TA) is a hydrophobic peptide isolated from the skin of the European red frog Rana temporaria. Strong antimicrobial activity against gram‐positive cocci and Candida, as well as its small molecular weight (10–13 aa residues), makes TA an interesting antimicrobial compound. However, its synthesis is rather problematic. Here, the synthesis of two retro‐analogues of TA – retro‐TA and (6‐1)(7‐13)‐TA—is reported. The synthesis of retro‐TA was performed without any problems, while during the synthesis of (6–1)(7–13)‐TA problems similar to those encountered during the synthesis of TA were faced. Antimicrobial assays showed minimal inhibitory concentration (MIC) values of retro‐TA to be, in most cases, only one dilution higher than those of original TA, but still remained relatively low. An analysis of the circular dichroism spectra of the peptides shows that TA and (6‐1)(7‐13)‐TA adopt an α‐helical structure in a hydrophobic environment, while retro‐TA forms mainly unordered conformation under both hydrophobic and hydrophilic conditions. One can postulate that differences in conformation of the peptide chain might be responsible for the lower antimicrobial activity of retro‐TA as compared to that of the parent molecule. In any case, retro‐TA can be interesting owing to its simple and nonproblematic synthesis. Copyright © 2006 European Peptide Society and John Wiley & Sons, Ltd.