title: Mechanical properties that influence antimicrobial peptide activity in lipid membranes.
abstract: Antimicrobial peptides are small amphiphilic proteins found in animals and plants as essential components of the innate immune system and whose function is to control bacterial infectious activity. In order to accomplish their function, antimicrobial peptides use different mechanisms of action which have been deeply studied in view of their potential exploitation to treat antibiotic-resistant bacterial infections. One of the main mechanisms of action of these peptides is the disruption of the bacterial membrane through pore formation, which, in some cases, takes place via a monomer to oligomer cooperative transition. Previous studies have shown that lipid composition, and the presence of exogenous components, such as cholesterol in model membranes or carotenoids in bacteria, can affect the potency of distinct antimicrobial peptides. At the same time, considering the membrane as a two-dimensional material, it has been shown that membrane composition defines its mechanical properties which might be relevant in many membrane-related processes. Nevertheless, the correlation between the mechanical properties of the membrane and antimicrobial peptide potency has not been considered according to the importance it deserves. The relevance of these mechanical properties in membrane deformation due to peptide insertion is reviewed here for different types of pores in order to elucidate if indeed membrane composition affects antimicrobial peptide activity by modulation of the mechanical properties of the membrane. This would also provide a better understanding of the mechanisms used by bacteria to overcome antimicrobial peptide activity.
authors.affiliation: Departamento de Física, Universidad de los Andes, Carrera 1 No. 18A-12, Bogota, Colombia. nmarin@uniandes.edu.co.
authors.forename: Nathaly
authors.initials: N
authors.lastname: Marín-Medina
authors.affiliation: Departamento de Física, Universidad de los Andes, Carrera 1 No. 18A-12, Bogota, Colombia.
authors.forename: Diego Alejandro
authors.initials: DA
authors.lastname: Ramírez
authors.affiliation: Departamento de Física, Universidad de los Andes, Carrera 1 No. 18A-12, Bogota, Colombia.
authors.forename: Steve
authors.initials: S
authors.lastname: Trier
authors.affiliation: Departamento de Física, Universidad de los Andes, Carrera 1 No. 18A-12, Bogota, Colombia.
authors.forename: Chad
authors.initials: C
authors.lastname: Leidy
mesh_terms: D000890:Anti-Infective Agents / Q000737:chemistry* / Q000378:metabolism*; D023181:Antimicrobial Cationic Peptides / Q000737:chemistry* / Q000378:metabolism*; D055598:Chemical Phenomena; D008051:Lipid Bilayers / Q000737:chemistry*; D008565:Membrane Proteins / Q000378:metabolism*
chemical_list: D000890:Anti-Infective Agents; D023181:Antimicrobial Cationic Peptides; D008051:Lipid Bilayers; D008565:Membrane Proteins
keywords: Antimicrobial peptides; Lipid membranes; Mechanical properties; Resistant bacteria