Two distinct amphipathic peptide antibiotics with systemic efficacy.
Publication/Presentation Date
8-11-2020
Abstract
Antimicrobial peptides are important candidates for developing new classes of antibiotics because of their potency against antibiotic-resistant pathogens. Current research focuses on topical applications and it is unclear how to design peptides with systemic efficacy. To address this problem, we designed two potent peptides by combining database-guided discovery with structure-based design. When bound to membranes, these two short peptides with an identical amino acid composition can adopt two distinct amphipathic structures: A classic horizontal helix (horine) and a novel vertical spiral structure (verine). Their horizontal and vertical orientations on membranes were determined by solid-state
Volume
117
Issue
32
First Page
19446
Last Page
19454
ISSN
1091-6490
Published In/Presented At
Lakshmaiah Narayana, J., Mishra, B., Lushnikova, T., Wu, Q., Chhonker, Y. S., Zhang, Y., Zarena, D., Salnikov, E. S., Dang, X., Wang, F., Murphy, C., Foster, K. W., Gorantla, S., Bechinger, B., Murry, D. J., & Wang, G. (2020). Two distinct amphipathic peptide antibiotics with systemic efficacy. Proceedings of the National Academy of Sciences of the United States of America, 117(32), 19446–19454. https://doi.org/10.1073/pnas.2005540117
Disciplines
Medicine and Health Sciences
PubMedID
32723829
Department(s)
Department of Pathology and Laboratory Medicine
Document Type
Article