Antimicrobial peptides AMPs

Line shape analysis of the static 31P NMR spectra and its corresponding CSA values have been successfully used to study the perturbation effect induced by proteins. 31P data for PLs bilayers interacting with antimicrobial peptide (AMP) magainin-2, aurein-3,3, incorporated into structures of supramolecular lipid assemblies such as toroidal pores and thinned bilayers have been reported.90 Various types of PL systems (l-palmitoyl-d3i-2-oleoyl-s -glycero-3-phosphotidylcholine... 

Two model peptides—alamethicin which is a-helix peptaibol-transmembrane antimicrobial peptide (AMP) and synthetic a-helix alanine-rich peptide (K3A18K3)—inserted into l,2-dimyristoyl-sn-glycero-3-phosphatidylcholine... 

A peptide (DPI), comprised of a protein transduction domain fused to an antimicrobial peptide (AMP) KLAKLAKKLAKLAK, triggered apoptosis in murine fibrosarcoma (MCA205) and human head and neck tumor cell lines in vitro. It also induced tumor apoptosis and reduction of tumor volume (MCA205) by direct intratumor injection [245]. 

Membrane-active antimicrobial peptides (AMPs), or host-defense peptides, kill microorganisms by permeabilizing their membrane. They often form amphipathic structures upon binding to lipid membranes. At low peptide concentrations they are normally in a monomeric surface-bound S-state, and at higher concentrations they may self-assemble and insert into the bilayer in a functionally active T- or I-state (see Figures 18.1 and 18.3). In our previous 19F NMR investigations we have compared three such AMPs, which are described below. 

Peptides are long, continuous and unbranched chain polymers formed by the polymerisation of amino acid monomers. During the polymerisation process two units are linked together via a peptide bond (-CO-NH-), which is formed by the reaction of a carboxylic group (-COOH) of one amino acid and an amino group (-NHi) of another. Peptides naturally occur in animals and plants, and can also be synthesised in the laboratory. Peptides play a significant role in the prevention of bacterial infections and, to date, more than 5,000 antimicrobial peptides (AMP) have been discovered or synthesised. 

Many organisms, from invertebrates to humans, rely on conserved cationic amphipathic oligopeptide sequences to augment the immune system [105]. These antimicrobial peptides (AMPs) are secreted by immune cells to serve as first-line, broad-spectrum antibiotics [105]. Cationic AMPs associate with negatively charged bacterial membranes. 

Antimicrobial peptides (AMPs) are currently among the promising agents for the treatments of infection. They are the main components of innate immunity and... 

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