Open AccessSelectively screen the antibacterial peptide from the hydrolysates of highland barley
Author(s) -
Pei Jinjin,
Feng Zhenzhen,
Ren Ting,
Jin Wengang,
Li Xinsheng,
Chen Dejing,
Tao Yanduo,
Dang Jun
Publication year - 2018
Publication title -
engineering in life sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.547
H-Index - 57
eISSN - 1618-2863
pISSN - 1618-0240
DOI - 10.1002/elsc.201700118
Subject(s) - hydrolysate , antibacterial activity , peptide , bacillus subtilis , escherichia coli , circular dichroism , peptide sequence , trypsin , hydrolysis , biochemistry , chemistry , liposome , biology , chromatography , bacteria , enzyme , gene , genetics
Highland barley is one of the most important industrial crops in Tibetan plateau. Previous research indicated that highland barley has many medical functions. In this work, the antibacterial abilities of highland barley were investigated. The protein solutions hydrolyzed by trypsin for 4 h exhibited the highest antibacterial activity. An antibacterial peptide, barleycin, was screened and purified by magnetic liposome extraction combining with the protein profiles of reversed‐phase high‐performance liquid chromatography (RP‐HPLC). Structure, characterization, and safety evaluation of barleycin were further investigated. Amino acids sequence was determined as Lys‐Ile‐Ile‐Ile‐Pro‐Pro‐Leu‐Phe‐His by N‐sequencing. Circular dichroism spectra indicated the a‐helix conformation of barleycin. The activity spectrum included Bacillus subtilis, Staphylcoccus aureus, Listeria innocua and Escherichia coli and the MICs were from 4 to 16 μg/mL. Safety evaluations with cytotoxicity and hemolytic suggested this antibacterial peptide could be considered as safe at MICs. Finally, mode of action of barleycin on sensitive cells was primarily studied. The results suggested the damage of cell membrane.