Action of antimicrobial peptides: two-state model.

By Huey W. Huang. Biochemistry, 2000

733 citations recorded by the source corpus.

Subfields: Microbiology, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/d4b9f51c453fe7a2a0b34bb0fbf394ed3223cff5

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Citations in the corpus

Melittin: a Membrane-active Peptide with Diverse Functions (2007, background): “…with respect to the membrane surface whereas when the concentration of peptide increases above a certain threshold value, an increasing fraction of peptide molecules change to the perpendicular orientation as explained by the two-state model for the action of antimicrobial peptides (Huang 2000).”
The Roles of Antimicrobial Peptides in Innate Host Defense (2009, background): “During the peptide-membrane interaction two physically distinct states occur [75].”
Barrel-stave model or toroidal model? A case study on melittin pores. (2001, background): “In lipid bilayers we have found variables that can switch the peptides from the inactive to the active state or vice versa (Huang, 2000).”
Role of membranes in the activities of antimicrobial cationic peptides. (2002, background): “Oriented circular dichroism [24], modelling, and depth-dependent quenching of tryptophan £uorescence [7] are all consistent with the conclusion that these peptides, regardless of structure, adopt a position at the interface of the lipid head groups and fatty acyl chains, parallel to the surface of t”
Defensins: antimicrobial peptides of innate immunity (2003, background): “Most biophysical studies on the mode of action of antimicrobial peptides have used simple α-helical (for example, magainin and cecropin) or β-loop (for example, protegrin) peptide”
Antimicrobial peptides: pore formers or metabolic inhibitors in bacteria? (2005, background): “In vitro studies of antimicrobial peptides incubated with single or mixed lipids in membranes or vesicles show that peptides bind in two physically distinct state”