RRC ID 38815
著者 Shin SY, Shimizu M, Ohtaki T, Munekata E.
タイトル Synthesis and biological activity of N-terminal-truncated derivatives of human epidermal growth factor (h-EGF).
ジャーナル Peptides
Abstract To investigate the contribution of the N-terminal sequence of h-EGF to its biological activity and the formation of three intramolecular disulfide bonds by oxidative refolding via air oxidation, five derivatives of h-EGF with a single N-terminal amino acid deletion were synthesized by solid-phase synthesis. The homogeneity of the synthetic peptides was confirmed by analytical reversed-phase HPLC, amino acid analysis, and FAB-MS. The pairing of the three disulfide bridges in synthetic peptides was determined by thermolytic digestion. All N-truncated derivatives of h-FGF formed the correct intramolecular three disulfide linkages during oxidative refolding and had equipotent activity in both EGF receptor binding on A-431 epidermoid carcinoma cells and mitogenesis on NIH-3T3 fibroblast cells, compared with authentic h-EGF. The results suggested that the five residues from N-terminal sequence of h-EGF have no effect on the formation of the correct disulfide linkages in h-EGF and do not exert a significant influence on its biological activity.
巻・号 16(2)
ページ 205-10
公開日 1995-1-1
DOI 10.1016/0196-9781(94)00181-2
PII 0196-9781(94)00181-2
PMID 7784250
MeSH 3T3 Cells Amino Acid Sequence Animals Binding, Competitive Carcinoma, Squamous Cell Cell Division / drug effects Chromatography, High Pressure Liquid Cysteine Dose-Response Relationship, Drug Epidermal Growth Factor / chemical synthesis* Epidermal Growth Factor / chemistry Epidermal Growth Factor / pharmacology* ErbB Receptors / metabolism* Humans Indicators and Reagents Kinetics Mice Molecular Sequence Data Peptide Fragments / chemical synthesis* Peptide Fragments / chemistry Peptide Fragments / pharmacology* Protein Conformation Protein Folding Tumor Cells, Cultured
IF 2.843
引用数 7
WOS 分野 PHARMACOLOGY & PHARMACY BIOCHEMISTRY & MOLECULAR BIOLOGY ENDOCRINOLOGY & METABOLISM
リソース情報
ヒト・動物細胞 A431(RCB0202)