Antibacterial activity identification of pCM19 and pCM12 derived from hGlyrichin.

Jibin Sha,Chenggang Zhang

doi:10.1186/s40064-016-3025-4

Jibin Sha, Chenggang Zhang

Open Access

https://doi.org/10.1186/s40064-016-3025-4

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Journal: SpringerPlus	Publication Date: Aug 22, 2016
Citations: 1	License type: CC BY 4.0

Affiliation: Shandong Sport University, Beijing Radiation Center

Abstract

BackgroundhGlyrichin is a novel human antimicrobial peptide rich in glycine. The previous study of known human antimicrobial peptides indicated that in an eligible range, the greater corresponding antibacterial activity was consisted with the shorter peptide sequence.FindingsTwo peptides named pCM19 and pCM12 were synthesized and the antibacterial activity assay results showed that these peptides exhibited strong antibacterial activity that was inversely proportional to the length of the peptide. Despite the effective inhibition of bacterial growth, the synthetic peptides showed no hemolytic effect on human red blood cells.ConclusionsTaken together, these two peptides derived from hGlyrichin both have strong antibacterial activity and are not toxic to human somatic cells.

Highlights

HGlyrichin is a novel human antimicrobial peptide rich in glycine
Taken together, these two peptides derived from hGlyrichin both have strong antibacterial activity and are not toxic to human somatic cells
The antibacterial activity identification and comparison of the peptide pCM19 and pCM12 Analysis of antibacterial activity based on bacteria colony counting As shown in Fig. 1, the pCM19 and pCM12 peptides effectively inhibited the growth of both Gram-negative bacterium

Summary

Introduction

HGlyrichin is a novel human antimicrobial peptide rich in glycine. The previous study of known human antimicrobial peptides indicated that in an eligible range, the greater corresponding antibacterial activity was consisted with the shorter peptide sequence. By comparing the sequences of the defensin family from plants, insects, birds, mammals, and other species, Yount and Yeaman identified a highly conserved threedimensional structure containing disulfide bonds, known as the γ core motif (Yeaman and Yount 2003). This special bi-directional amino acid sequence motif contains two anti-parallel β-sheet structures and a short coil insert sequence, and exists in all species, suggesting that the defensins from different species may be derived from a common precursor (Ganz 2003; Selsted and Ouellette 2005). The results suggest that the γ core motif may be the functional domain of the defensin family

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