title: Lipopolysaccharide induces amyloid formation of antimicrobial peptide HAL-2.
abstract: Lipopolysaccharide (LPS), the important component of the outer membrane of Gram-negative bacteria, contributes to the integrity of the outer membrane and protects the cell against bactericidal agents, including antimicrobial peptides. However, the mechanisms of interaction between antimicrobial peptides and LPS are not clearly understood. Halictines-2 (HAL-2), one of the novel antimicrobial peptides, was isolated from the venom of the eusocial bee Halictus sexcinctus. HAL-2 has exhibited potent antimicrobial activity against Gram-positive and Gram-negative bacteria and even against cancer cells. Here, we studied the interactions between HAL-2 and LPS to elucidate the antibacterial mechanism of HAL-2 in vitro. Our results show that HAL-2 adopts a significant degree of β-strand structure in the presence of LPS. LPS is capable of inducing HAL-2 amyloid formation, which may play a vital role in its antimicrobial activity.
authors.affiliation: High Magnetic Field Laboratory, Hefei Institutes of Physical Science, Chinese Academy of Science, Hefei, Anhui 230031, PR China.
authors.forename: Jiarong
authors.initials: J
authors.lastname: Wang
authors.affiliation: High Magnetic Field Laboratory, Hefei Institutes of Physical Science, Chinese Academy of Science, Hefei, Anhui 230031, PR China.
authors.forename: Yan
authors.initials: Y
authors.lastname: Li
authors.affiliation: High Magnetic Field Laboratory, Hefei Institutes of Physical Science, Chinese Academy of Science, Hefei, Anhui 230031, PR China.
authors.forename: Xiaoming
authors.initials: X
authors.lastname: Wang
authors.affiliation: High Magnetic Field Laboratory, Hefei Institutes of Physical Science, Chinese Academy of Science, Hefei, Anhui 230031, PR China.
authors.forename: Wei
authors.initials: W
authors.lastname: Chen
authors.affiliation: High Magnetic Field Laboratory, Hefei Institutes of Physical Science, Chinese Academy of Science, Hefei, Anhui 230031, PR China. Electronic address: hbsun@hmfl.ac.cn.
authors.forename: Hongbin
authors.initials: H
authors.lastname: Sun
authors.affiliation: High Magnetic Field Laboratory, Hefei Institutes of Physical Science, Chinese Academy of Science, Hefei, Anhui 230031, PR China. Electronic address: junfeng@hmfl.ac.cn.
authors.forename: Junfeng
authors.initials: J
authors.lastname: Wang
keywords: Aggregation; Amyloid formation; Antimicrobial peptide; HAL-2; NMR spectroscopy