Work

Investigating the nucleic acid interactions of histone‐derived antimicrobial peptides

Year: 2017

Type: article

Abstract: While many antimicrobial peptides (AMPs) disrupt bacterial membranes, some translocate into bacteria and interfere with intracellular processes. Buforin II and DesHDAP1 are thought to kill bacteria by interacting with nucleic acids. Here, molecular modeling and experimental measurements are used to show that neither nucleic acid binding peptide selectively binds DNA sequences. Simulations and experiments also show that changing lysines to arginines enhances DNA binding, suggesting that including additional guanidinium groups is a potential strategy to engineer more potent AMPs. Moreover, the lack of binding specificity may make it more difficult for bacteria to evolve resistance to these and other similar AMPs.

Source: FEBS Letters

DOI: 10.1002/1873-3468.12574

Authors: Sukin Sim, Penny Wang, Brittany N. Beyer, Kara J. Cutrona, Mala L. Radhakrishnan, Donald E. Elmore

Institution: Wellesley College

Language: English

Topic: Antimicrobial Peptides and Activities

Subfield: Microbiology

Field: Immunology and Microbiology

Domain: Life Sciences

Open Access status: green

Funders: National Science Foundation, National Institute of Allergy and Infectious Diseases, National Center for Research Resources, Division of Chemistry

Awards: RUI: A Systematic, Computational Study of the Effect of Macromolecular Crowding on Electrostatic Interactions, Biomolecular Recognition, and Molecular Design, REU Site: Chemistry as the Focus of an Interdisciplinary Summer Research Program at Wellesley College, Characterization and Design of Histone-Derived Antimicrobial Peptides, High Performance Computing for Biomedical Research