R
Richard M. Epand
Researcher at McMaster University
Publications - 521
Citations - 26937
Richard M. Epand is an academic researcher from McMaster University. The author has contributed to research in topics: Membrane & Peptide. The author has an hindex of 80, co-authored 515 publications receiving 25125 citations. Previous affiliations of Richard M. Epand include Brigham Young University & University of Edinburgh.
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Journal ArticleDOI
Diversity of antimicrobial peptides and their mechanisms of action.
Richard M. Epand,Hans J. Vogel +1 more
TL;DR: It is not likely that this diverse group of peptides has a single mechanism of action, but interaction of the peptides with membranes is an important requirement for most, if not all, antimicrobial peptides.
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Lipid domains in bacterial membranes and the action of antimicrobial agents.
Richard M. Epand,Raquel F. Epand +1 more
TL;DR: Interestingly many antimicrobial agents are polycationic and therefore likely have some effect in promoting lipid phase segregation between anionic and zwitterionic lipids, but this mechanism is expected to be most important for substances with sequential positive charges contained within a flexible molecule.
Journal ArticleDOI
Relationship of membrane curvature to the formation of pores by magainin 2.
Katsumi Matsuzaki,Ken’ichi Sugishita,Noriko Ishibe,Mayu Ueha,Saori Nakata,Koichiro Miyajima,Richard M. Epand +6 more
TL;DR: It is suggested that the peptide imposes positive curvature strain, facilitating the formation of a torus-type pore, and that the presence of negative curvature-inducing lipids inhibits pore formation.
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Bacterial lipid composition and the antimicrobial efficacy of cationic steroid compounds (Ceragenins).
TL;DR: The antimicrobial action of the ceragenins correlates better with the content of phosphatidylethanolamine in the bacterial membrane than whether or not the bacteria has an outer membrane, suggesting that the bacterial lipid composition can be an important factor in determining the sensitivity of bacteria to antimicrobial agents.
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Mimicry of antimicrobial host-defense peptides by random copolymers.
Brendan P. Mowery,Sarah E. Lee,Denis A. Kissounko,Raquel F. Epand,Richard M. Epand,Bernard Weisblum,Shannon S. Stahl,Samuel H. Gellman +7 more
TL;DR: It is shown that random poly-β-peptide copolymers, prepared by ring-opening polymerization of β-lactams, can be tuned to display good activity against a panel of four bacteria along with low lytic activity toward human red blood cells, which support a nonclassical design hypothesis for antibacterial agents.