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Synthesis and Biological Activity of Seleno Sunflower Trypsin Inhibitor Analog
Author(s) -
Guo Xin,
Shi Jiahao,
Tang Zhenyu,
Cui Dafu,
Zhang Youshang
Publication year - 2006
Publication title -
chemical biology and drug design
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.59
H-Index - 77
eISSN - 1747-0285
pISSN - 1747-0277
DOI - 10.1111/j.1747-0285.2006.00457.x
Subject(s) - sunflower , trypsin inhibitor , chemistry , biological activity , trypsin , biochemistry , biology , enzyme , agronomy , in vitro
Sunflower trypsin inhibitor (SFTI‐1) is a cyclic peptide with 14 amino acid residues and one disulfide bond. Its synthetic acyclic analog (aSFTI‐1) with N‐terminal Gly and C‐terminal Asp was still active. Here, we report the synthesis of seleno aSFTI‐1 with the disulfide bond of aSFTI‐1 replaced by diselenide bond. The formation of the diselenide bond from selenol was achieved in a single step without the aid of oxidizing agent. For comparison, aSFTI‐1 itself and aSFTI‐1 with its disulfide bond replaced by two serines ([Ser 3,11 ] aSFTI‐1) were also synthesized. The trypsin inhibitory constants of seleno aSFTI‐1, aSFTI‐1 and [Ser 3,11 ] aSFTI‐1 were determined as 6.50 × 10 −9 , 1.96 × 10 −9 and 8.10 × 10 −6 respectively, indicating that the disulfide bond is essential for the structure and function of aSFTI‐1, and seleno aSFTI‐1 is still active, although its inhibitory constant is reduced to 30% in comparison with that of aSFTI‐1.