Interaction between amphiphilic peptides and phospholipid membranes

• Published in: Current opinion in colloid & interface science Vol. 15; no. 6; pp. 467 - 478
• Main Authors: Strömstedt, Adam A., Ringstad, Lovisa, Schmidtchen, Artur, Malmsten, Martin
• Format: Journal Article
• Language: English
• Published: Amsterdam Elsevier Ltd 01.12.2010; Elsevier
• Subjects: Adsorption; AMP; Antimicrobial peptide; Bacteria; Charge; Chemical Sciences; Chemistry; Colloidal state and disperse state; Density; Exact sciences and technology; FARMACI; Focusing; Fysikalisk kemi; General and physical chemistry; Hydrophobicity; Kemi; Liposome; Membrane; Membranes; Natural Sciences; Naturvetenskap; Peptides; PHARMACY; Phospholipids; Physical Chemistry; Surface physical chemistry; Liposome; Bacteria; Membrane; AMP; Antimicrobial peptide; Composition; Correlation; Stability; Peptides; Membrane interaction; Phospholipid; Review; Hydrophobicity; Topology; Density; Cholesterol; Adsorption; Focusing; Models; Structure
• ISSN: 1359-0294; 1879-0399; 1879-0399
• DOI: 10.1016/j.cocis.2010.05.006

This brief review aims at providing some illustrative examples on the interaction between amphiphilic peptides and phospholipid membranes, an area of significant current interest. Focusing on antimicrobial peptides, factors affecting peptide–membrane interactions are addressed, including effects of peptide length, charge, hydrophobicity, secondary structure, and topology. Effects of membrane composition are also illustrated, including effects of membrane charge, nature of the polar headgroup, and presence of cholesterol and other sterols. Throughout, novel insights on the importance of peptide adsorption density on membrane stability are emphasized, as is the correlation between peptide adsorption, peptide-induced leakage in model liposome systems, peptide-induced lysis of bacteria, and bacteria killing. Figure caption: Amphiphilic peptides interact with phospholipid membranes and may cause membrane destabilization, such as that observed for antimicrobial peptides. Through controlling peptide adsorption characteristics, selective membrane interactions may be reached, so that membranes of bacteria and other pathogens are disrupted, while those of human cells are left relatively unperturbed. [Display omitted]