A novel peptide from Apis mellifera and solid-phase synthesis of its analogue
Yu Meng, Xiao Xiao Yang, Yu Xin Sheng, Jin Lan Zhang, De Quan Yu, Chinese Chem. Lett., 2012, 23, 1161â€“1164.
Copyright © 2012 De Quan Yu. Published by Elsevier B.V. All rights reserved.
A novel peptide designated secapin-1, was purified and characterized from Apis mellifera. The molecular weight of 25 amino acid peptide secapin-1 was found to be 2821.5625 Da by ESI-FTICR-MS. It showed high identity to secapin. The sequence of secapin-1 was determined to be YIINVPPRCPPGSKFVKNKCRVIVP by automatic Edman degradation. A disulfide bond was formed between Cys9 and Cys20 residues. In addition, an analogue of secapin-1 was synthesized by solid phase peptide synthesis method. The synthesis product was successfully purified and identified to homogeneity by using a combination of SEC, IEC, and RP-HPLC techniques.