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- W2390721851 abstract "We reported the properties and bacteriostatic mechanism of the antimicrobial peptide R-1from marine Brevibacillus laterosporus.R-1 was very stable to keep the antibacterial activity even after incubation at 121 ℃ and in the pH rang of 11.0~12.0 for 1 hours.In addition,R-1 was insensitive to trypsin,chymotrypsin,and alkaline proteinase.R-1 activity was slightly enhanced by Ba2+,Li+,Mg2+,Mn2+,Fe2+,Cu2+,Sr2+,Pb2+,Zn2+,and Ca2+.R-1 showed good compatibility to many common chemical reagents,including EDTA and KH2PO4.Tween and SDS showed obvious effects.Amino acid analysis of R-1 showed that R-1 was composed of Leu,Tyr,Val,Ile,Lys,Gly,Met,Ser,and Ala.R-1 had broad-spectrum against many bacteria including a number of pathogens.Observation by scanning electron microscopy suggested that the bioactivity mechanism of R-1 lied in pertoration of cell membrane,leading to bacterium lysis and death." @default.
- W2390721851 created "2016-06-24" @default.
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- W2390721851 date "2010-01-01" @default.
- W2390721851 modified "2023-09-25" @default.
- W2390721851 title "Properties and bacteriostatic mechanism of the antimicrobial peptide R-1" @default.
- W2390721851 hasPublicationYear "2010" @default.
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