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Structure-function relationship of antimicrobial peptide cathelicidin Pc-CATH1

DOI: 10.1007/s13659-012-0016-1

Keywords: cathelicidin,antimicrobial peptide,structure-function relationship

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Abstract:

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.

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