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Titolo:
Sequences of polypeptide antibiotics stilboflavins, natural peptaibol libraries of the mold Stilbella flavipes
Autore:
Jaworski, A; Bruckner, H;
Indirizzi:
Univ Giessen, Dept Food Sci, Inst Nutrit Sci, Interdisciplinary Res Ctr, D-35392 Giessen, Germany Univ Giessen Giessen Germany D-35392 y Res Ctr, D-35392 Giessen, Germany
Titolo Testata:
JOURNAL OF PEPTIDE SCIENCE
fascicolo: 8, volume: 7, anno: 2001,
pagine: 433 - 447
SICI:
1075-2617(200108)7:8<433:SOPASN>2.0.ZU;2-V
Fonte:
ISI
Lingua:
ENG
Soggetto:
ALPHA-AMINOISOBUTYRIC-ACID; FUNGUS TRICHODERMA-HARZIANUM; HYPELCIN-A-III; MASS-SPECTROMETRY; STRUCTURAL ELUCIDATION; HEMOLYTIC PROPERTIES; PARACELSIN PEPTIDES; FILAMENTOUS FUNGI; HYPOCREA-PELTATA; METABOLITES;
Keywords:
alpha-aminoisobutyric acid (Aib); electrospray ionization mass spectrometry; peptide antibiotics; peptaibol library; sequence analysis; Stilbella flavipes; stilboflavins;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
51
Recensione:
Indirizzi per estratti:
Indirizzo: Bruckner, H Univ Giessen, Dept Food Sci, Inst Nutrit Sci, Interdisciplinary Res Ctr, Heinrich Buff Ring 26-32, D-35392 Giessen, Germany Univ Giessen Heinrich Buff Ring 26-32 Giessen Germany D-35392
Citazione:
A. Jaworski e H. Bruckner, "Sequences of polypeptide antibiotics stilboflavins, natural peptaibol libraries of the mold Stilbella flavipes", J PEPT SCI, 7(8), 2001, pp. 433-447

Abstract

From the culture broths of the mold Stilbella flavipes CBS 146.81, a mixture of polypeptides could be isolated by adsorption on XAD polystyrene resinand purified by Sephadex LH-20 chromatography. Using preparative thin-layer chromatography (TLC) three groups of peptides, named stilboflavins (SF) A, B, and C could be separated. Each of the groups showed microheterogeneitywhen investigated by high-performance liquid chromatography (HPLC). Employing on-line HPLC-electrospray ionization tandem mass spectrometry in the positive and negative ionization mode, together with gas chromatography-selected ion monitoring mass spectrometry, enantioselective GC and quantitative amino acid analysis, the sequences of stilboflavins A and B could be determined. Exchange of Glu in stilboflavins A peptides (acidic) against Gln in stilboflavins A peptides (neutral) is the rational for different polarity ofthe peptide groups and their separatability by TLC. Since SF A and B are bioactive N-acetylated 20-residue peptides with a high proportion of alpha -aminoisobutyric acid and C-terminal bonded amino alcohols (either leucinol,isoleucinol or valinol) the peptides belong to the group of peptaibol antibiotics. Copyright (C) 2001 European Peptide Society and John Wiley & Sons,Ltd.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 04/04/20 alle ore 14:39:10