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. 2012 Mar 28;2(2):81–86. doi: 10.1007/s13659-012-0016-1

Structure-function relationship of antimicrobial peptide cathelicidin Pc-CATH1

Li Dong 1,3, Juan-Juan Yang 2, Ying Wang 1,3, Huan Liu 1, Li-Xian Mu 1,3, Dong-Hai Lin 2,✉, Ren Lai 1,✉
PMCID: PMC4131589

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. Inline graphic

Keywords: cathelicidin, antimicrobial peptide, structure-function relationship

Footnotes

These authors contributed equally to this work.

This article is published with open access at Springerlink.com

Contributor Information

Dong-Hai Lin, Email: dhlin@xmu.edu.cn.

Ren Lai, Email: rlai@mail.kiz.ac.cn.

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