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Titolo:
Identification and characterization of an antibacterial peptide of the 26-kDa protease of Sarcophaga peregrina with antibacterial activity
Autore:
Tsuji, Y; Aoyama, T; Takeuchi, K; Homma, K; Takahashi, H; Nakajima, Y; Shimada, I; Natori, S;
Indirizzi:
Inst Phys & Chem Res, Natori Special Lab, Wako, Saitama 3510198, Japan Inst Phys & Chem Res Wako Saitama Japan 3510198 o, Saitama 3510198, Japan Univ Tokyo, Grad Sch Pharmaceut Sci, Bunkyo Ku, Tokyo, Japan Univ Tokyo Tokyo Japan Grad Sch Pharmaceut Sci, Bunkyo Ku, Tokyo, Japan
Titolo Testata:
JOURNAL OF BIOCHEMISTRY
fascicolo: 2, volume: 130, anno: 2001,
pagine: 313 - 318
SICI:
0021-924X(200108)130:2<313:IACOAA>2.0.ZU;2-U
Fonte:
ISI
Lingua:
ENG
Soggetto:
LYSOSOMAL CATHEPSIN-G; FLESH-FLY; SARCOTOXIN-IA; HUMAN NEUTROPHILS; SERINE-PROTEASE; BACTERICIDAL ACTIVITY; MOLECULAR-CLONING; ESCHERICHIA-COLI; IMAGINAL DISKS; CDNA CLONING;
Keywords:
amphiphilic alpha-helix; antibacterial peptide; bacterial membrane; insect; serine protease;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
30
Recensione:
Indirizzi per estratti:
Indirizzo: Natori, S Inst Phys & Chem Res, Natori Special Lab, 2-1 Hirosawa, Wako, Saitama 3510198, Japan Inst Phys & Chem Res 2-1 Hirosawa Wako Saitama Japan 3510198 pan
Citazione:
Y. Tsuji et al., "Identification and characterization of an antibacterial peptide of the 26-kDa protease of Sarcophaga peregrina with antibacterial activity", J BIOCHEM, 130(2), 2001, pp. 313-318

Abstract

Previously, we purified a serine protease with a molecular mass of 26 kDa that exhibits potent antibacterial activity from a pupal extract of Sarcophaga peregrina (flesh fly). We divided this protease into 12 peptides and examined their antibacterial activity. A peptide corresponding to residues 155 to 174 (peptide 9) was found to exhibit antibacterial activity comparableto that of the 26-kDa protease. When Escherichia coli was treated with peptide 9, the permeability of both the outer and inner membranes increased, and substrates for beta -lactamase and beta -galactosidase entered the cells, but beta -galactosidase did not leak out of the cells under these conditions. It was suggested that residues 6 to 18 of peptide 9 form an amphiphilic a-helix under hydrophobic conditions with an N-terminal basic loop and then interact with acidic phospholipids in the bacterial membranes.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 03/07/20 alle ore 15:34:36