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Antibacterial mechanism of the Asp-Asp-Asp-Tyr peptide

Previously, we found that ASP-ASP-ASP-TYR (DDDY) from Dendrobium aphyllum has a minimum inhibitory concentration of 36.15 mg/mL against Pseudomonas aeruginosa. Here, we explored the antibacterial mechanism of DDDY and its potential preservation applications. Metabolomic and transcriptomic analyses r...

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Autores principales: Zhuang, Shanshan, Bao, Yao, Zhang, Yaxin, Zhang, Huangyou, Liu, Jianliang, Liu, Huifan
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9039886/
https://www.ncbi.nlm.nih.gov/pubmed/35499031
http://dx.doi.org/10.1016/j.fochx.2022.100229
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author Zhuang, Shanshan
Bao, Yao
Zhang, Yaxin
Zhang, Huangyou
Liu, Jianliang
Liu, Huifan
author_facet Zhuang, Shanshan
Bao, Yao
Zhang, Yaxin
Zhang, Huangyou
Liu, Jianliang
Liu, Huifan
author_sort Zhuang, Shanshan
collection PubMed
description Previously, we found that ASP-ASP-ASP-TYR (DDDY) from Dendrobium aphyllum has a minimum inhibitory concentration of 36.15 mg/mL against Pseudomonas aeruginosa. Here, we explored the antibacterial mechanism of DDDY and its potential preservation applications. Metabolomic and transcriptomic analyses revealed that DDDY mainly affects genes involved in P. aeruginosa membrane transport and amino acid metabolism pathways. Molecular dynamics simulation revealed that DDDY had a stronger effect on 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphoethanolamine phospholipid membranes than on 1-palmitoyl-2-oleoyl-lecithin or 1-palmitoyl-2-oleoyl phosphatidylglycerol membranes, with high DDDY concentrations displaying stronger efficacy on 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphoethanolamine. Mechanistically, the N-terminal of DDDY first bound to the phospholipid head group, while its C-terminal amino acid residue bound the hydrophobic tail, thereby creating a gap in the membrane when the phospholipids were clustered by hydrogen bonding. Finally, DDDY inhibited the growth of food microorganisms inoculated onto chestnut kernels, suggesting that DDDY is a promising antibacterial agent against multidrug-resistant gram-negative bacteria.
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spelling pubmed-90398862022-04-27 Antibacterial mechanism of the Asp-Asp-Asp-Tyr peptide Zhuang, Shanshan Bao, Yao Zhang, Yaxin Zhang, Huangyou Liu, Jianliang Liu, Huifan Food Chem X Article(s) from the Special Issue on Novel proteins and peptides for human consumption: sources, chemistry and function by Dr. González-Córdova and Dr. Sáyago-Ayerdi Previously, we found that ASP-ASP-ASP-TYR (DDDY) from Dendrobium aphyllum has a minimum inhibitory concentration of 36.15 mg/mL against Pseudomonas aeruginosa. Here, we explored the antibacterial mechanism of DDDY and its potential preservation applications. Metabolomic and transcriptomic analyses revealed that DDDY mainly affects genes involved in P. aeruginosa membrane transport and amino acid metabolism pathways. Molecular dynamics simulation revealed that DDDY had a stronger effect on 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphoethanolamine phospholipid membranes than on 1-palmitoyl-2-oleoyl-lecithin or 1-palmitoyl-2-oleoyl phosphatidylglycerol membranes, with high DDDY concentrations displaying stronger efficacy on 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphoethanolamine. Mechanistically, the N-terminal of DDDY first bound to the phospholipid head group, while its C-terminal amino acid residue bound the hydrophobic tail, thereby creating a gap in the membrane when the phospholipids were clustered by hydrogen bonding. Finally, DDDY inhibited the growth of food microorganisms inoculated onto chestnut kernels, suggesting that DDDY is a promising antibacterial agent against multidrug-resistant gram-negative bacteria. Elsevier 2022-01-29 /pmc/articles/PMC9039886/ /pubmed/35499031 http://dx.doi.org/10.1016/j.fochx.2022.100229 Text en © 2022 The Author(s) https://creativecommons.org/licenses/by-nc-nd/4.0/This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).
spellingShingle Article(s) from the Special Issue on Novel proteins and peptides for human consumption: sources, chemistry and function by Dr. González-Córdova and Dr. Sáyago-Ayerdi
Zhuang, Shanshan
Bao, Yao
Zhang, Yaxin
Zhang, Huangyou
Liu, Jianliang
Liu, Huifan
Antibacterial mechanism of the Asp-Asp-Asp-Tyr peptide
title Antibacterial mechanism of the Asp-Asp-Asp-Tyr peptide
title_full Antibacterial mechanism of the Asp-Asp-Asp-Tyr peptide
title_fullStr Antibacterial mechanism of the Asp-Asp-Asp-Tyr peptide
title_full_unstemmed Antibacterial mechanism of the Asp-Asp-Asp-Tyr peptide
title_short Antibacterial mechanism of the Asp-Asp-Asp-Tyr peptide
title_sort antibacterial mechanism of the asp-asp-asp-tyr peptide
topic Article(s) from the Special Issue on Novel proteins and peptides for human consumption: sources, chemistry and function by Dr. González-Córdova and Dr. Sáyago-Ayerdi
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9039886/
https://www.ncbi.nlm.nih.gov/pubmed/35499031
http://dx.doi.org/10.1016/j.fochx.2022.100229
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