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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...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Springer Berlin Heidelberg
2012
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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] |
format | Online Article Text |
id | pubmed-4131589 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2012 |
publisher | Springer Berlin Heidelberg |
record_format | MEDLINE/PubMed |
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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