Antimicrobial Activity of Small Synthetic Peptides Based on the Marine Peptide Turgencin A: Prediction of Antimicrobial Peptide Sequences in a Natural Peptide and Strategy for Optimization of Potency
Turgencin A, a potent antimicrobial peptide isolated from the Arctic sea squirt Synoicum turgens, consists of 36 amino acid residues and three disulfide bridges, making it challenging to synthesize. The aim of the present study was to develop a truncated peptide with an antimicrobial drug lead poten...
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ftmdpi:oai:mdpi.com:/1422-0067/21/15/5460/ 2023-08-20T04:04:20+02:00 Antimicrobial Activity of Small Synthetic Peptides Based on the Marine Peptide Turgencin A: Prediction of Antimicrobial Peptide Sequences in a Natural Peptide and Strategy for Optimization of Potency Ida K. Ø. Hansen Tomas Lövdahl Danijela Simonovic Kine Ø. Hansen Aaron J. C. Andersen Hege Devold Céline S. M. Richard Jeanette H. Andersen Morten B. Strøm Tor Haug agris 2020-07-30 application/pdf https://doi.org/10.3390/ijms21155460 EN eng Multidisciplinary Digital Publishing Institute Molecular Microbiology https://dx.doi.org/10.3390/ijms21155460 https://creativecommons.org/licenses/by/4.0/ International Journal of Molecular Sciences; Volume 21; Issue 15; Pages: 5460 Arctic ascidian antimicrobial synthetic peptide Synoicum turgens Text 2020 ftmdpi https://doi.org/10.3390/ijms21155460 2023-07-31T23:51:27Z Turgencin A, a potent antimicrobial peptide isolated from the Arctic sea squirt Synoicum turgens, consists of 36 amino acid residues and three disulfide bridges, making it challenging to synthesize. The aim of the present study was to develop a truncated peptide with an antimicrobial drug lead potential based on turgencin A. The experiments consisted of: (1) sequence analysis and prediction of antimicrobial potential of truncated 10-mer sequences; (2) synthesis and antimicrobial screening of a lead peptide devoid of the cysteine residues; (3) optimization of in vitro antimicrobial activity of the lead peptide using an amino acid replacement strategy; and (4) screening the synthesized peptides for cytotoxic activities. In silico analysis of turgencin A using various prediction software indicated an internal, cationic 10-mer sequence to be putatively antimicrobial. The synthesized truncated lead peptide displayed weak antimicrobial activity. However, by following a systematic amino acid replacement strategy, a modified peptide was developed that retained the potency of the original peptide. The optimized peptide StAMP-9 displayed bactericidal activity, with minimal inhibitory concentrations of 7.8 µg/mL against Staphylococcus aureus and 3.9 µg/mL against Escherichia coli, and no cytotoxic effects against mammalian cells. Preliminary experiments indicate the bacterial membranes as immediate and primary targets. Text Arctic MDPI Open Access Publishing Arctic International Journal of Molecular Sciences 21 15 5460 |
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MDPI Open Access Publishing |
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ftmdpi |
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English |
topic |
Arctic ascidian antimicrobial synthetic peptide Synoicum turgens |
spellingShingle |
Arctic ascidian antimicrobial synthetic peptide Synoicum turgens Ida K. Ø. Hansen Tomas Lövdahl Danijela Simonovic Kine Ø. Hansen Aaron J. C. Andersen Hege Devold Céline S. M. Richard Jeanette H. Andersen Morten B. Strøm Tor Haug Antimicrobial Activity of Small Synthetic Peptides Based on the Marine Peptide Turgencin A: Prediction of Antimicrobial Peptide Sequences in a Natural Peptide and Strategy for Optimization of Potency |
topic_facet |
Arctic ascidian antimicrobial synthetic peptide Synoicum turgens |
description |
Turgencin A, a potent antimicrobial peptide isolated from the Arctic sea squirt Synoicum turgens, consists of 36 amino acid residues and three disulfide bridges, making it challenging to synthesize. The aim of the present study was to develop a truncated peptide with an antimicrobial drug lead potential based on turgencin A. The experiments consisted of: (1) sequence analysis and prediction of antimicrobial potential of truncated 10-mer sequences; (2) synthesis and antimicrobial screening of a lead peptide devoid of the cysteine residues; (3) optimization of in vitro antimicrobial activity of the lead peptide using an amino acid replacement strategy; and (4) screening the synthesized peptides for cytotoxic activities. In silico analysis of turgencin A using various prediction software indicated an internal, cationic 10-mer sequence to be putatively antimicrobial. The synthesized truncated lead peptide displayed weak antimicrobial activity. However, by following a systematic amino acid replacement strategy, a modified peptide was developed that retained the potency of the original peptide. The optimized peptide StAMP-9 displayed bactericidal activity, with minimal inhibitory concentrations of 7.8 µg/mL against Staphylococcus aureus and 3.9 µg/mL against Escherichia coli, and no cytotoxic effects against mammalian cells. Preliminary experiments indicate the bacterial membranes as immediate and primary targets. |
format |
Text |
author |
Ida K. Ø. Hansen Tomas Lövdahl Danijela Simonovic Kine Ø. Hansen Aaron J. C. Andersen Hege Devold Céline S. M. Richard Jeanette H. Andersen Morten B. Strøm Tor Haug |
author_facet |
Ida K. Ø. Hansen Tomas Lövdahl Danijela Simonovic Kine Ø. Hansen Aaron J. C. Andersen Hege Devold Céline S. M. Richard Jeanette H. Andersen Morten B. Strøm Tor Haug |
author_sort |
Ida K. Ø. Hansen |
title |
Antimicrobial Activity of Small Synthetic Peptides Based on the Marine Peptide Turgencin A: Prediction of Antimicrobial Peptide Sequences in a Natural Peptide and Strategy for Optimization of Potency |
title_short |
Antimicrobial Activity of Small Synthetic Peptides Based on the Marine Peptide Turgencin A: Prediction of Antimicrobial Peptide Sequences in a Natural Peptide and Strategy for Optimization of Potency |
title_full |
Antimicrobial Activity of Small Synthetic Peptides Based on the Marine Peptide Turgencin A: Prediction of Antimicrobial Peptide Sequences in a Natural Peptide and Strategy for Optimization of Potency |
title_fullStr |
Antimicrobial Activity of Small Synthetic Peptides Based on the Marine Peptide Turgencin A: Prediction of Antimicrobial Peptide Sequences in a Natural Peptide and Strategy for Optimization of Potency |
title_full_unstemmed |
Antimicrobial Activity of Small Synthetic Peptides Based on the Marine Peptide Turgencin A: Prediction of Antimicrobial Peptide Sequences in a Natural Peptide and Strategy for Optimization of Potency |
title_sort |
antimicrobial activity of small synthetic peptides based on the marine peptide turgencin a: prediction of antimicrobial peptide sequences in a natural peptide and strategy for optimization of potency |
publisher |
Multidisciplinary Digital Publishing Institute |
publishDate |
2020 |
url |
https://doi.org/10.3390/ijms21155460 |
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agris |
geographic |
Arctic |
geographic_facet |
Arctic |
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Arctic |
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Arctic |
op_source |
International Journal of Molecular Sciences; Volume 21; Issue 15; Pages: 5460 |
op_relation |
Molecular Microbiology https://dx.doi.org/10.3390/ijms21155460 |
op_rights |
https://creativecommons.org/licenses/by/4.0/ |
op_doi |
https://doi.org/10.3390/ijms21155460 |
container_title |
International Journal of Molecular Sciences |
container_volume |
21 |
container_issue |
15 |
container_start_page |
5460 |
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1774714729405612032 |