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Structure-function relationship of antimicrobial peptide cathelicidin Pc-CATH1

Cathelicidin Pc-CATH1 is a cathelicidin-derived myeloid antimicrobial peptide identified from Phasianus colchicus with strong antimicrobial activity against most of bacteria and fungi tested, including the clinically isolated (IS) drug-resistant strains. Considering the uniform distribution of net p...

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Detalles Bibliográficos
Autores principales: Dong, Li, Yang, Juan-Juan, Wang, Ying, Liu, Huan, Mu, Li-Xian, Lin, Dong-Hai, Lai, Ren
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Springer Berlin Heidelberg 2012
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4131589/
http://dx.doi.org/10.1007/s13659-012-0016-1
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author Dong, Li
Yang, Juan-Juan
Wang, Ying
Liu, Huan
Mu, Li-Xian
Lin, Dong-Hai
Lai, Ren
author_facet Dong, Li
Yang, Juan-Juan
Wang, Ying
Liu, Huan
Mu, Li-Xian
Lin, Dong-Hai
Lai, Ren
author_sort Dong, Li
collection PubMed
description Cathelicidin Pc-CATH1 is a cathelicidin-derived myeloid antimicrobial peptide identified from Phasianus colchicus with strong antimicrobial activity against most of bacteria and fungi tested, including the clinically isolated (IS) drug-resistant strains. Considering the uniform distribution of net positive charge in both C- and N-terminus sequence of cathelicidin Pc-CATH1 and most of hydrophobic amino acid (aa) residues positioned in middle of the sequence, the antimicrobial peptide was used to investigate the structure-function relationship by truncating gradually N- or C-terminus amino acid residue. More than 10 modified peptide homologues (20–26 aa length) of cathelicidin Pc-CATH1 were found to keep strong antimicrobial abilities. The possible relationships between bioactivities including antimicrobial and hemolytic abilities, components of secondary structure, hydrophobicity, amphipathicity, net charge, and sequence length were investigated. The current work provided suggestions for structural and functional modification of linear, α-helical antimicrobial peptides containing no disulfided bridges. [Image: see text]
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spelling pubmed-41315892014-08-20 Structure-function relationship of antimicrobial peptide cathelicidin Pc-CATH1 Dong, Li Yang, Juan-Juan Wang, Ying Liu, Huan Mu, Li-Xian Lin, Dong-Hai Lai, Ren Nat Prod Bioprospect Regular Article Cathelicidin Pc-CATH1 is a cathelicidin-derived myeloid antimicrobial peptide identified from Phasianus colchicus with strong antimicrobial activity against most of bacteria and fungi tested, including the clinically isolated (IS) drug-resistant strains. Considering the uniform distribution of net positive charge in both C- and N-terminus sequence of cathelicidin Pc-CATH1 and most of hydrophobic amino acid (aa) residues positioned in middle of the sequence, the antimicrobial peptide was used to investigate the structure-function relationship by truncating gradually N- or C-terminus amino acid residue. More than 10 modified peptide homologues (20–26 aa length) of cathelicidin Pc-CATH1 were found to keep strong antimicrobial abilities. The possible relationships between bioactivities including antimicrobial and hemolytic abilities, components of secondary structure, hydrophobicity, amphipathicity, net charge, and sequence length were investigated. The current work provided suggestions for structural and functional modification of linear, α-helical antimicrobial peptides containing no disulfided bridges. [Image: see text] Springer Berlin Heidelberg 2012-03-28 /pmc/articles/PMC4131589/ http://dx.doi.org/10.1007/s13659-012-0016-1 Text en © The Author(s) 2012
spellingShingle Regular Article
Dong, Li
Yang, Juan-Juan
Wang, Ying
Liu, Huan
Mu, Li-Xian
Lin, Dong-Hai
Lai, Ren
Structure-function relationship of antimicrobial peptide cathelicidin Pc-CATH1
title Structure-function relationship of antimicrobial peptide cathelicidin Pc-CATH1
title_full Structure-function relationship of antimicrobial peptide cathelicidin Pc-CATH1
title_fullStr Structure-function relationship of antimicrobial peptide cathelicidin Pc-CATH1
title_full_unstemmed Structure-function relationship of antimicrobial peptide cathelicidin Pc-CATH1
title_short Structure-function relationship of antimicrobial peptide cathelicidin Pc-CATH1
title_sort structure-function relationship of antimicrobial peptide cathelicidin pc-cath1
topic Regular Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4131589/
http://dx.doi.org/10.1007/s13659-012-0016-1
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