Literature DB >> 36151500

Probing the Functional Interaction Interface of Lipopolysaccharide and Antimicrobial Peptides: A Solution-State NMR Perspective.

Karishma Biswas1, Anirban Bhunia2.   

Abstract

Antimicrobial peptides (AMPs) have been a topic of substantial research as the next-generation antibiotics. They have been extensively studied for the selectivity and action against microbial membrane lipids in imparting their targeted functioning. To determine the effectivity of the peptides against the Gram-negative pathogens, it is imperative to elucidate their role in interacting with the lipopolysaccharide moieties. Lipopolysaccharide is a major component of the outer membrane of the Gram-negative bacteria. It serves to protect the bacteria as well as govern the functionality of several antibacterial agents. It can prevent the access of the agents into the inner membrane of the bacteria, thus rendering them inactive. Several techniques have been employed to study the interaction for better designing of peptides; NMR spectroscopy is one of the most widely used techniques in determining the interactive properties of peptides with LPS as it can provide the details in atomistic level. NMR spectroscopy provides information about the structural and conformational changes as well as the dynamics of the interactions.
© 2022. The Author(s), under exclusive license to Springer Science+Business Media, LLC, part of Springer Nature.

Entities:  

Keywords:  Antimicrobial peptides; Lipopolysaccharide; NMR spectroscopy; Saturation transfer difference NMR; Transferred NOESY

Mesh:

Substances:

Year:  2022        PMID: 36151500     DOI: 10.1007/978-1-0716-2581-1_13

Source DB:  PubMed          Journal:  Methods Mol Biol        ISSN: 1064-3745


  57 in total

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10.  Lipopolysaccharide, a key molecule involved in the synergism between temporins in inhibiting bacterial growth and in endotoxin neutralization.

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Journal:  J Biol Chem       Date:  2008-06-12       Impact factor: 5.157

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