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Titolo:
Androctonin, a hydrophilic disulphide-bridged non-haemolytic anti-microbial peptide: a plausible mode of action
Autore:
Hetru, C; Letellier, L; Oren, Z; Hoffmann, JA; Shai, Y;
Indirizzi:
Inst Biol Mol & Cellulaire, UPR 9022 CNRS, F-67084 Strasbourg, France InstBiol Mol & Cellulaire Strasbourg France F-67084 Strasbourg, France Univ Paris Sud, Lab Biomembranes, UMR 8619 CNRS, F-91405 Orsay, France Univ Paris Sud Orsay France F-91405 UMR 8619 CNRS, F-91405 Orsay, France Weizmann Inst Sci, Dept Biol Chem, IL-76100 Rehovot, Israel Weizmann Inst Sci Rehovot Israel IL-76100 Chem, IL-76100 Rehovot, Israel
Titolo Testata:
BIOCHEMICAL JOURNAL
, volume: 345, anno: 2000,
parte:, 3
pagine: 653 - 664
SICI:
0264-6021(20000201)345:<653:AAHDNA>2.0.ZU;2-O
Fonte:
ISI
Lingua:
ENG
Soggetto:
TRANSFORM INFRARED-SPECTROSCOPY; ESCHERICHIA-COLI-CELLS; ANTIMICROBIAL PEPTIDES; ANTIBACTERIAL PEPTIDE; PHOSPHOLIPID-MEMBRANES; SECONDARY STRUCTURE; INSECT DEFENSIN; TACHYPLESIN-I; CECROPIN P1; ANTIBIOTICS;
Keywords:
fluorescent spectroscopy; lipid-peptide interaction; scorpion;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
57
Recensione:
Indirizzi per estratti:
Indirizzo: Hetru, C Inst Biol Mol & Cellulaire, UPR 9022 CNRS, 15 Rue Rene Descartes,F-67084 Strasbourg, France Inst Biol Mol & Cellulaire 15 Rue Rene Descartes Strasbourg France F-67084
Citazione:
C. Hetru et al., "Androctonin, a hydrophilic disulphide-bridged non-haemolytic anti-microbial peptide: a plausible mode of action", BIOCHEM J, 345, 2000, pp. 653-664

Abstract

Androctonin is a 25-residue non-haemolytic anti-microbial peptide isolatedfrom the scorpion Androctonus australis and contains two disulphide bridges. Androctonin is different from known native anti-microbial peptides, being a relatively hydrophilic and non-amphipathic molecule. This raises the possibility that the target of androctonin might not be the bacterial membrane, shown to be a target for most amphipathic lytic peptides. To shed light on its mode of action on bacteria and its nonhaemolytic activity, we synthesized androctonin, its fluorescent derivatives and its all-D-amino acid enantiomer. The enantiomer preserved high activity, suggesting a lipid-peptideinteraction between androctonin and bacterial membranes. In Gram-positive and (at higher concentrations) Gram-negative bacteria, androctonin induced an immediate perturbation of the permeability properties of the cytoplasmicmembrane of the bacterial energetic state, concomitant with perturbation of the morphology of the cell envelope as revealed by electron microscopy. Androctonin binds only to negatively charged lipid vesicles and induces the leakage of markers at high concentrations and with a slow kinetics, in contrast with amphipathic alpha-helical anti-microbial peptides that bind and permeate negatively charged vesicles, and to a smaller extent also zwitterionic ones. This might explain the selective lytic activity of androctonin towards bacteria but not red blood cells. Polarized attenuated total reflection-Fourier transform infrared spectroscopy revealed that androctonin adoptsa beta-sheet structure in membranes and did not affect the lipid acyl chain order, which supports a detergent-like effect. The small size of androctonin, its hydrophilic character and its physicochemical properties are favourable features for its potential application as a replacement for commercially available antibiotics to which bacteria have developed resistance.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 01/12/20 alle ore 21:42:54