Novel non-helical antimicrobial peptides insert into and fuse lipid model membranes

This journal contribution is published Open Access by the publisher. Follow the DOI link to retrieve a copy of the full text. This work is based upon research conducted at the Center for High Energy X-ray Sciences (CHEXS at CHESS), which is supported by the National Science Foundation under award DMR-1829070, and the Macromolecular Diffraction at CHESS (MacCHESS) facility, which is supported by award 1-P30-GM124166-01A1 from the National Institute of General Medical Sciences, National Institutes of Health, and by New York State's Empire State Development Corporation (NYSTAR). Additional support for this work was from the National Science Foundation (NSF) MCB-2115790 (S. M., S. T-N.), National Institute of Allergy and Infectious Diseases (NIAID) 1R01AI172861-01A1 (B. D., S. T-N.). Bhairavi Chandersekhar was supported by Carnegie Mellon University SURF program, and Yunshu Li by the Robert Kramer Award at CMU Physics. F. H. was supported by the U.S. Department of Commerce (award 70NANB17H299). The content of this publication does not necessarily reflect the views or policies of the Department of Health and Human Services, nor does mention of trade names, commercial products, or organizations imply endorsement by the U.S. Government. B. K. was supported by the Danish Agency for Science, Technology and Innovation (DanScatt). The authors would like to acknowledge the ISIS facility at Rutherford Appleton Laboratory, Harwell Campus, U.K, doi:10.5286/ISIS.E.RB2310027, and the Materials Characterization Facility Xenocs Xeuss 3.0, Carnegie Mellon University, funded by the NSF Major Research Instrumentation (MRI) award CMMI-2117523. The authors would also like to acknowledge Dr Richard Gillilan for his help at CHEXS (CHESS).