Cargando…
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...
Autores principales: | , , , , , |
---|---|
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 |
_version_ | 1784694225501159424 |
---|---|
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. |
format | Online Article Text |
id | pubmed-9039886 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | Elsevier |
record_format | MEDLINE/PubMed |
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 |
work_keys_str_mv | AT zhuangshanshan antibacterialmechanismoftheaspaspasptyrpeptide AT baoyao antibacterialmechanismoftheaspaspasptyrpeptide AT zhangyaxin antibacterialmechanismoftheaspaspasptyrpeptide AT zhanghuangyou antibacterialmechanismoftheaspaspasptyrpeptide AT liujianliang antibacterialmechanismoftheaspaspasptyrpeptide AT liuhuifan antibacterialmechanismoftheaspaspasptyrpeptide |