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Titolo:
Synthetic peptides derived from the beta(2)-beta(3) loop of Raphanus sativus antifungal protein 2 that mimic the active site
Autore:
Schaaper, WMM; Posthuma, GA; Plasman, HH; Sijtsma, L; Fant, F; Borremans, FAM; Thevissen, K; Broekaert, WF; Meloen, RH; van Amerongen, A;
Indirizzi:
Inst Anim Sci & Hlth, ID Lelystad, Dept Mol Recognit, NL-8200 AB Lelystad,Netherlands Inst Anim Sci & Hlth Lelystad Netherlands NL-8200 AB elystad,Netherlands Agrotechnol Res Inst, ATO, Wageningen, Netherlands Agrotechnol Res Inst Wageningen Netherlands TO, Wageningen, Netherlands State Univ Ghent, Dept Organ Chem, B-9000 Ghent, Belgium State Univ GhentGhent Belgium B-9000 Organ Chem, B-9000 Ghent, Belgium Katholieke Univ Leuven, Genet Lab, B-3001 Heverlee, Belgium Katholieke Univ Leuven Heverlee Belgium B-3001 B-3001 Heverlee, Belgium
Titolo Testata:
JOURNAL OF PEPTIDE RESEARCH
fascicolo: 5, volume: 57, anno: 2001,
pagine: 409 - 418
SICI:
1397-002X(200105)57:5<409:SPDFTB>2.0.ZU;2-#
Fonte:
ISI
Lingua:
ENG
Soggetto:
3-DIMENSIONAL SOLUTION STRUCTURE; INSECT DEFENSIN-A; PLANT DEFENSINS; ANTIMICROBIAL PEPTIDES; FUNGAL GROWTH; BINDING-SITES; PERMEABILIZATION; INHIBITION; ENDOSPERM; MEMBRANES;
Keywords:
alpha-aminobutyric acid; AFP; antifungal peptides; beta-sheet; cyclic disulfide; loop peptide;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
28
Recensione:
Indirizzi per estratti:
Indirizzo: Schaaper, WMM Inst Anim Sci & Hlth, ID Lelystad, Dept Mol Recognit, POB 65, NL-8200 AB Lelystad, Netherlands Inst Anim Sci & Hlth POB 65 Lelystad Netherlands NL-8200 AB
Citazione:
W.M.M. Schaaper et al., "Synthetic peptides derived from the beta(2)-beta(3) loop of Raphanus sativus antifungal protein 2 that mimic the active site", J PEPT RES, 57(5), 2001, pp. 409-418

Abstract

Rs-AFPs are antifungal proteins, isolated from radish (Raphanus sativus) seed or leaves, which consist of 50 or 51 amino acids and belong to the plant defensin family of proteins. Four highly homologous Rs-AFPs have been isolated (Rs-AFP1-4). The structure of Rs-AFP1 consists of three beta -strandsand an alpha -helix, and is stabilized by four cystine bridges. Small peptides deduced from the native sequence, still having biological activity, are not only important tools to study structure-function relationships, but may also constitute a commercially interesting target. In an earlier study, we showed that the antifungal activity of Rs-AFP2 is concentrated mainly inthe beta2-beta3 loop. In this study, we synthesized linear 19-mer peptides, spanning the entire beta2-beta3 loop, that were found to be almost as potent as Rs-AFP2. Cysteines, highly conserved in the native protein, are essential for maintaining the secondary structure of the protein. Surprisingly,in the 19-mer loop peptides, cysteines can be replaced by alpha -aminobutyric acid, which even improves the antifungal potency of the peptides. Analogous cyclic 19-mer peptides, forced to adopt a hairpin structure by the introduction of one or two non-native disulfide bridges, were also found to possess high antifungal activity. The synthetic 19-mer peptides, like Rs-AFP2itself, cause increased Ca2+ influx in pregerminated fungal hyphae.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 22/01/20 alle ore 12:41:23