Bulletin of ANPA

Abstract submitted to ANPA Conference July 14–16, 2023

Volume 5, Number 1

Biological, Medical, Soft Matter and Chemical Physics

Abstract ID: ANPA2023-N00033

Abstract:

ANPA2023-N00033: Multimeric Assembly and Membrane Pore Forming Dynamics of the Lantibiotic Peptide Nisin

Authors:

• Hugo Perez; Florida International University

• Prem Chapagain; Florida International University

• Jin He;

Multidrug resistance in bacteria has led to a dire need for the development of new antibiotics with novel modes of action which can evade existing bacterial defenses. By targeting Lipid-II, antibiotic peptides such as Nisin disrupt bacteria’s ability to synthesize their cell wall. Lantibiotics bind to Lipid-II’s pyrophosphate moiety rather than the more commonly targeted peptide moiety. This means that bacteria that develop resistance to commercial antibiotics should still be vulnerable to lantibiotics. In this study, we use atomic-scale molecular dynamics computational studies to model stable oligomeric pore structures of nisin and investigate their dynamics and stability. We test a variety of conformations of nisin pore structures and motifs to find a viable structure. We also explore the role that Lipid-II plays in the formation and in maintaining the stability of the pores as well as the role transmembrane potentials play in the nature of the pores, including the channel volume and the ability of Nisin pores to exhibit ion selectivity.

To cite this abstract, use the following reference: https://anpaglobal.org/conference/2023/ANPA2023-N00033