Abstract
Lipopolysaccharide (LPS) plays a critical role in the pathogenesis of sepsis caused by gram-negative bacterial infections. Therefore, LPS-neutralizing molecules would have important clinical applications. Chensinin-1, a novel antimicrobial peptide with atypical structural features, was found in the skin secretions of the Chinese brown frog Rana chensinensis. To understand the role of LPS in the bacterial susceptibility to chensinin-1 and to investigate its anti-endotoxin effects, the interactions of chensinin-1 with LPS were investigated in this study using circular dichroism, in situ IR, isothermal titration calorimetry, and zeta potential. This study is the first to use in situ IR spectroscopy to evaluate the secondary structural changes of this peptide. The capacity of chensinin-1 to block the LPS-dependent cytokine secretion of macrophages was also investigated. Our results show that chensinin-1 can form α-helical structures in LPS suspensions. LPS can affect the antimicrobial activity of chensinin-1, and chensinin-1 was able to mitigate the effects of LPS. These data may facilitate the development of antimicrobial peptides with potent antimicrobial and anti-endotoxin activities.
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Citations
Apr 10, 2016·Acta Biomaterialia·Weibing DongDejing Shang
Nov 4, 2016·Pharmaceuticals·Erum MalikDavid A Phoenix
Jan 6, 2017·Scientific Reports·Weibing DongDejing Shang
Feb 15, 2019·Scientific Reports·Simone C BarbosaOsvaldo N Oliveira
Jan 12, 2020·Journal of Fluorescence·Weibing DongDejing Shang
Aug 6, 2020·Antibiotics·Daisuke OgawaShawichi Iwamuro
Jan 27, 2021·Molecular Immunology·Juan ZhangDejing Shang