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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...

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Autores principales: Yang, Hao, Fu, Jingyu, Zhao, Youyun, Shi, Huiping, Hu, Hua, Wang, Hongliang
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
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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.
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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
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