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Investigating the nucleic acid interactions of histone‐derived antimicrobial peptides
Author(s) -
Sim Sukin,
Wang Penny,
Beyer Brittany N.,
Cutrona Kara J.,
Radhakrishnan Mala L.,
Elmore Donald E.
Publication year - 2017
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.12574
Subject(s) - nucleic acid , antimicrobial peptides , biochemistry , dna , bacteria , peptide , histone , antimicrobial , biology , chemistry , intracellular , microbiology and biotechnology , genetics
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.