Investigating the nucleic acid interactions of histone‐derived antimicrobial peptides. Issue 5 (1st March 2017)

• Record Type: Journal Article
• Authors: Sim, Sukin; Wang, Penny; Beyer, Brittany N.; Cutrona, Kara J.; Radhakrishnan, Mala L.; Elmore, Donald E.
• Is Part Of: FEBS letters. Volume 591:Issue 5(2017)
• Page Start: 706
• Page End: 717
• Publication Date: 2017-03-01
• Subjects: antimicrobial peptide -- electrostatics calculations -- molecular dynamics -- nucleic acid; Biochemistry -- Periodicals; Biophysics -- Periodicals; Molecular biology -- Periodicals; Biochimie -- Périodiques; Biochemistry; Biophysics; Molecular biology; Periodicals; 572.05
• DOI: 10.1002/1873-3468.12574
• Languages: English
• ISSNs: 0014-5793

Abstract

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. Abstract :