Temporin A and its retro-analogues: synthesis, conformational analysis and antimicrobial activities
(2006) In Journal of Peptide Science 12(8). p.533-537- Abstract
- 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... (More)
- 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 alpha-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. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/1135396
- author
- Kamysz, Wojciech ; Mickiewicz, Beata ; Rodziewicz-Motowidlo, Sylwia ; Greber, Katarzyna and Okroj, Marcin LU
- publishing date
- 2006
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- antimicrobial peptides, peptide synthesis, circular dichroism
- in
- Journal of Peptide Science
- volume
- 12
- issue
- 8
- pages
- 533 - 537
- publisher
- John Wiley & Sons Inc.
- external identifiers
-
- pmid:16724306
- scopus:33747241354
- ISSN
- 1099-1387
- DOI
- 10.1002/psc.762
- language
- English
- LU publication?
- no
- id
- 52dbdb7b-a620-4aa1-b3c7-3a9ba7c17f52 (old id 1135396)
- date added to LUP
- 2016-04-01 12:07:57
- date last changed
- 2022-01-26 23:14:08
@article{52dbdb7b-a620-4aa1-b3c7-3a9ba7c17f52,
abstract = {{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 alpha-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.}},
author = {{Kamysz, Wojciech and Mickiewicz, Beata and Rodziewicz-Motowidlo, Sylwia and Greber, Katarzyna and Okroj, Marcin}},
issn = {{1099-1387}},
keywords = {{antimicrobial peptides; peptide synthesis; circular dichroism}},
language = {{eng}},
number = {{8}},
pages = {{533--537}},
publisher = {{John Wiley & Sons Inc.}},
series = {{Journal of Peptide Science}},
title = {{Temporin A and its retro-analogues: synthesis, conformational analysis and antimicrobial activities}},
url = {{http://dx.doi.org/10.1002/psc.762}},
doi = {{10.1002/psc.762}},
volume = {{12}},
year = {{2006}},
}