Cargando…
Escherichia Coli PagP Enzyme-Based De Novo Design and In Vitro Activity of Antibacterial Peptide LL-37
BACKGROUND: The aim of this study was to investigate the antimicrobial property of peptide LL-37 sequences. MATERIAL/METHODS: Humanized antibacterial peptide LL-37 and the mutant were prepared by chemical synthesis. The physicochemical properties of antibacterial peptide LL-37 were analyzed by SWISS...
Autores principales: | , , , , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
International Scientific Literature, Inc.
2017
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5458668/ https://www.ncbi.nlm.nih.gov/pubmed/28550277 http://dx.doi.org/10.12659/MSM.902095 |
_version_ | 1783241804578029568 |
---|---|
author | Yang, Hao Fu, Jingyu Zhao, Youyun Shi, Huiping Hu, Hua Wang, Hongliang |
author_facet | Yang, Hao Fu, Jingyu Zhao, Youyun Shi, Huiping Hu, Hua Wang, Hongliang |
author_sort | Yang, Hao |
collection | PubMed |
description | BACKGROUND: The aim of this study was to investigate the antimicrobial property of peptide LL-37 sequences. MATERIAL/METHODS: Humanized antibacterial peptide LL-37 and the mutant were prepared by chemical synthesis. The physicochemical properties of antibacterial peptide LL-37 were analyzed by SWISS-MODEL online prediction tool. Molecular docking between antibacterial peptide LL-37 fragments and palmitoyl transferase PagP was made with Lamarckian genetic algorithm by AutoDock1.5.6. RESULTS: The systems contacted each other at 8.75 picosec. After 20 picsec, the system had no trend of dissociation, and the bond energy of weak bond -C-O-H…NH2-CH2- was calculated. The hydrophobic groups were important factors that led to contact and merged the two parts. The contacted weak bond -C-O-H…NH2-CH2- was the bridge for contacting LL-37 with palmitoyl transferase PagP. The binding sites of antibacterial peptide LL-37 and palmitoyl transferase PagP mainly included LYS8, GLU11, LEU28, LYS12, PHE27, ILE13, and PHE6 of antibacterial peptide LL-37 and ARG94, TRP89, ASN65, SER3, GLU90, GLU90, ASN100, HIS102, and THR92 of palmitoyl transferase PagP. CONCLUSIONS: Antibacterial peptide LL-37 had stronger antibacterial effect via inhibition of activity of PagP. |
format | Online Article Text |
id | pubmed-5458668 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | International Scientific Literature, Inc. |
record_format | MEDLINE/PubMed |
spelling | pubmed-54586682017-06-13 Escherichia Coli PagP Enzyme-Based De Novo Design and In Vitro Activity of Antibacterial Peptide LL-37 Yang, Hao Fu, Jingyu Zhao, Youyun Shi, Huiping Hu, Hua Wang, Hongliang Med Sci Monit Lab/In Vitro Research BACKGROUND: The aim of this study was to investigate the antimicrobial property of peptide LL-37 sequences. MATERIAL/METHODS: Humanized antibacterial peptide LL-37 and the mutant were prepared by chemical synthesis. The physicochemical properties of antibacterial peptide LL-37 were analyzed by SWISS-MODEL online prediction tool. Molecular docking between antibacterial peptide LL-37 fragments and palmitoyl transferase PagP was made with Lamarckian genetic algorithm by AutoDock1.5.6. RESULTS: The systems contacted each other at 8.75 picosec. After 20 picsec, the system had no trend of dissociation, and the bond energy of weak bond -C-O-H…NH2-CH2- was calculated. The hydrophobic groups were important factors that led to contact and merged the two parts. The contacted weak bond -C-O-H…NH2-CH2- was the bridge for contacting LL-37 with palmitoyl transferase PagP. The binding sites of antibacterial peptide LL-37 and palmitoyl transferase PagP mainly included LYS8, GLU11, LEU28, LYS12, PHE27, ILE13, and PHE6 of antibacterial peptide LL-37 and ARG94, TRP89, ASN65, SER3, GLU90, GLU90, ASN100, HIS102, and THR92 of palmitoyl transferase PagP. CONCLUSIONS: Antibacterial peptide LL-37 had stronger antibacterial effect via inhibition of activity of PagP. International Scientific Literature, Inc. 2017-05-27 /pmc/articles/PMC5458668/ /pubmed/28550277 http://dx.doi.org/10.12659/MSM.902095 Text en © Med Sci Monit, 2017 This work is licensed under Creative Common Attribution-NonCommercial-NoDerivatives 4.0 International (CC BY-NC-ND 4.0 (https://creativecommons.org/licenses/by-nc-nd/4.0/) ) |
spellingShingle | Lab/In Vitro Research Yang, Hao Fu, Jingyu Zhao, Youyun Shi, Huiping Hu, Hua Wang, Hongliang Escherichia Coli PagP Enzyme-Based De Novo Design and In Vitro Activity of Antibacterial Peptide LL-37 |
title | Escherichia Coli PagP Enzyme-Based De Novo Design and In Vitro Activity of Antibacterial Peptide LL-37 |
title_full | Escherichia Coli PagP Enzyme-Based De Novo Design and In Vitro Activity of Antibacterial Peptide LL-37 |
title_fullStr | Escherichia Coli PagP Enzyme-Based De Novo Design and In Vitro Activity of Antibacterial Peptide LL-37 |
title_full_unstemmed | Escherichia Coli PagP Enzyme-Based De Novo Design and In Vitro Activity of Antibacterial Peptide LL-37 |
title_short | Escherichia Coli PagP Enzyme-Based De Novo Design and In Vitro Activity of Antibacterial Peptide LL-37 |
title_sort | escherichia coli pagp enzyme-based de novo design and in vitro activity of antibacterial peptide ll-37 |
topic | Lab/In Vitro Research |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5458668/ https://www.ncbi.nlm.nih.gov/pubmed/28550277 http://dx.doi.org/10.12659/MSM.902095 |
work_keys_str_mv | AT yanghao escherichiacolipagpenzymebaseddenovodesignandinvitroactivityofantibacterialpeptidell37 AT fujingyu escherichiacolipagpenzymebaseddenovodesignandinvitroactivityofantibacterialpeptidell37 AT zhaoyouyun escherichiacolipagpenzymebaseddenovodesignandinvitroactivityofantibacterialpeptidell37 AT shihuiping escherichiacolipagpenzymebaseddenovodesignandinvitroactivityofantibacterialpeptidell37 AT huhua escherichiacolipagpenzymebaseddenovodesignandinvitroactivityofantibacterialpeptidell37 AT wanghongliang escherichiacolipagpenzymebaseddenovodesignandinvitroactivityofantibacterialpeptidell37 |