Journal
JOURNAL OF PEPTIDE SCIENCE
Volume 21, Issue 6, Pages 454-460Publisher
WILEY-BLACKWELL
DOI: 10.1002/psc.2756
Keywords
small protein; NPGL; microwave; solid-phase peptide synthesis; disulfide bond formation
Funding
- MEXT/JSPS KAKENHI [22687004, 26291066, 25440171]
- Toray Science Foundation
- Program for Promotion of Basic and Applied Researches for Innovations in Bio-oriented Industry
- Grants-in-Aid for Scientific Research [26291066, 14J05738, 22687004, 25440171] Funding Source: KAKEN
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We recently identified a novel cDNA encoding a small secretory protein of 80 amino acid residues, termed neurosecretory protein GL (NPGL), from the chicken hypothalamus. Homologs of NPGL have been reported to be present in mammals, such as human and rat. NPGL is amidated at its C-terminus, contains an intramolecular disulfide bond, and is hydrophobic in nature. In this study, we have optimized the synthesis of the entire 80-amino acid peptide sequence of rat NPGL by microwave-assisted solid-phase peptide synthesis. NPGL was obtained with a 10% yield when the coupling reactions were performed using 1-[Bis(dimethylamino)methylene]-1H-1,2,3-triazolo[4,5-b]pyridinium-3-oxid hexafluorophosphate (HATU) at 50 degrees C for 5min, and Fmoc deprotections were performed using 40% piperidine containing 0.1M HOBt. Furthermore, the disulfide bond of NPGL was formed with 20% yield with the use of glutathione-containing redox buffer and 50% acetonitrile. Copyright (c) 2015 European Peptide Society and John Wiley & Sons, Ltd.
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