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Titolo:
Characterization of unique amphipathic antimicrobial peptides from venom of the scorpion Pandinus imperator
Autore:
Corzo, G; Escoubas, P; Villegas, E; Barnham, KJ; He, WL; Norton, RS; Nakajima, T;
Indirizzi:
Suntory Inst Bioorgan Res, Shimamoto, Osaka 6188503, Japan Suntory Inst Bioorgan Res Shimamoto Osaka Japan 6188503 ka 6188503, Japan Suntory Inst Fundamental Res, Shimamoto, Osaka 6180001, Japan Suntory InstFundamental Res Shimamoto Osaka Japan 6180001 6180001, Japan Biomol Res Inst, Parkville, Vic 3052, Australia Biomol Res Inst ParkvilleVic Australia 3052 rkville, Vic 3052, Australia
Titolo Testata:
BIOCHEMICAL JOURNAL
, volume: 359, anno: 2001,
parte:, 1
pagine: 35 - 45
SICI:
0264-6021(20011001)359:<35:COUAAP>2.0.ZU;2-8
Fonte:
ISI
Lingua:
ENG
Soggetto:
ANTIBACTERIAL PEPTIDE; SOLUTION CONFORMATION; CHEMICAL-SHIFTS; MODEL MEMBRANES; FROG; NMR; SKIN; MELITTIN; SEQUENCE; H-1-NMR;
Keywords:
alpha-helical peptides; arthropod venom; haemolytic activity;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
54
Recensione:
Indirizzi per estratti:
Indirizzo: Corzo, G Suntory Inst Bioorgan Res, Wakayamadai 1-1-1, Shimamoto, Osaka 6188503, Japan Suntory Inst Bioorgan Res Wakayamadai 1-1-1 Shimamoto Osaka Japan 6188503
Citazione:
G. Corzo et al., "Characterization of unique amphipathic antimicrobial peptides from venom of the scorpion Pandinus imperator", BIOCHEM J, 359, 2001, pp. 35-45

Abstract

Two novel antimicrobial peptides have been identified and characterized from venom of the African scorpion Pandinus imperator. The peptides, designated pandinin 1 and 2, are alpha -helical polycationic peptides, with pandinin 1 belonging to the group of antibacterial peptides previously described from scorpions, frogs and insects. and pandinin 2 to the group of short magainin-type helical peptides from frogs. Both peptides demonstrated high antimicrobial activity against a range of Grampositive bacteria (2.4-5.2 muM). but were less active against Gram-negative bacteria (2.4-38.2 muM), and only pandinin 2 affected the yeast Candida albicans, Pandinin 2 also demonstrated strong haemolytic activity (11.1-44.5 muM) against sheep erythrocytes, in contrast with pandinin 1, which was not haemolytic. CD studies and a high-resolution structure of pandinin 2 determined by NMR, showed that the twopeptides are both essentially helical, but differ in their overall structure. Pandinin 2 is composed of a single alpha -helix with a predominantly hydrophobic N-terminal sequence. whereas pandinin 1 consists of two distinct a-helices separated by a coil region of higher flexibility, This is the first report of magainin-type polycationic antimicrobial peptides in scorpion venom. Their presence brings new insights into the mode of action of scorpion venom and also opens new avenues for the discovery of novel antibiotic molecules from arthropod venoms.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 25/06/18 alle ore 17:22:11