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Titolo:
CHEMICAL SYNTHESIS OF DENDROTOXIN-I - REVISION OF THE REPORTED STRUCTURE
Autore:
NISHIO H; INUI T; NISHIUCHI Y; DEMEDEIROS CLC; ROWAN EG; HARVEY AL; KATOH E; YAMAZAKI T; KIMURA T; SAKAKIBARA S;
Indirizzi:
PEPTIDE INST INC,PROT RES FDN,4-1-2 INA OSAKA 562 JAPAN PEPTIDE INST INC,PROT RES FDN OSAKA 562 JAPAN UNIV STRATHCLYDE,STRATHCLYDE INST DRUG RES GLASGOW G1 1XW LANARK SCOTLAND UNIV STRATHCLYDE,DEPT PHYSIOL & PHARMACOL GLASGOW G1 1XW LANARK SCOTLAND NATL INST AGROBIOL RESOURCES TSUKUBA IBARAKI 305 JAPAN
Titolo Testata:
The journal of peptide research
fascicolo: 5, volume: 51, anno: 1998,
pagine: 355 - 364
SICI:
1397-002X(1998)51:5<355:CSOD-R>2.0.ZU;2-C
Fonte:
ISI
Lingua:
ENG
Soggetto:
PROTEASE INHIBITOR HOMOLOGS; SNAKE-VENOM TOXINS; BLACK MAMBA VENOM; POTASSIUM CHANNELS; ALPHA-DENDROTOXIN; H-1-NMR SPECTRA; PURIFICATION; SPECTROSCOPY; PEPTIDE; ASSIGNMENT;
Keywords:
CHEMICAL SYNTHESIS; DENDROTOXIN I; NMR ANALYSIS; POTASSIUM CHANNEL BLOCKER; RECEPTOR BINDING ASSAY; REVISED STRUCTURE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
22
Recensione:
Indirizzi per estratti:
Citazione:
H. Nishio et al., "CHEMICAL SYNTHESIS OF DENDROTOXIN-I - REVISION OF THE REPORTED STRUCTURE", The journal of peptide research, 51(5), 1998, pp. 355-364

Abstract

Dendrotoxin I (DTX-I) is a 60-residue peptide from the venom of the black mamba snake Dendroaspis polylepis. which binds to neuronal K+ channels. The structure reported previously for DTX-I was synthesized forthe first time by a solution procedure. The synthetic product was confirmed to have the correct primary and disulfide structure determined by peptide mapping, sequence analysis and mass measurements. Comparison of synthetic DTX-I with the natural one by high-performance liquid chromatography and capillary zone electrophoresis, as well as by sequence analysis, revealed that the Asn residue at position 12 in the synthetic peptide was Asp in the natural product. Synthesis of DTX-I with Asp at position 12 gave a peptide identical with the natural product inall aspects. NMR analysis of synthetic [Asn(12)]- and [Asp(12)]-DTX-Ialso supported our findings that the Asn residue at position 12 in the DTX-I molecule should be revised as Asp. [Asn(12)]- and [Asp(12)]-DTX-I had very similar binding affinities when tested against radiolabeled dendrotoxin binding to rat brain synaptosomal membranes. (C) Munksgaard 1998.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 10/07/20 alle ore 09:48:47