A novel angiotensin converting enzyme inhibitory peptide derived from proteolytic digest of Chinese soft-shelled turtle egg white proteins

in Sciences Citation Index(SCI), 科學引文索引資料庫(SCI)
標題A novel angiotensin converting enzyme inhibitory peptide derived from proteolytic digest of Chinese soft-shelled turtle egg white proteins
出版類型SCI(Sciences Citation Index)
出版年度2013
AuthorsReynetha D.S. Rawendra, 藍文卓, Aisha 何艾莎, Chang 張誌益, 奧拉妮, Ho-Hsien Chen 陳和賢, Tzou-Chi Huang 黃卓治, & Liao Ming-Huei 徐睿良
開始頁359
頁數10
出版日期2013 / 10
其他編號NSC 98-2113-M-020 -002 -MY2
中文摘要

In this study, soft-shelled turtle (Pelodiscus sinensis) egg white (SSTEW) proteins were
digested by thermolysin and the resulting small peptides were further fractionated by
reverse phase chromatography. Peptides with angiotensin I-converting enzyme inhibitory
(ACEI) activity from these fractions were screened. A lysozyme-derived peptide, IW-11, from
the fraction with the most effective ACEI was identified by liquid chromatography–tandem
mass spectrometry (LC–MS/MS) and its purified form showed effective ACEI activity in vitro
(IC50 = 4.39 ± 0.31 μM). The Lineweaver–Burk plots indicated that the inhibition towards
ACE caused by this peptide is a competitive inhibition. The molecular docking study further
revealed that the ACEI activity of IW-11 is mainly attributed to the formation of hydrogen
bonds between the N-terminal residue of IW-11 and the S1 pocket (Ala354 and Tyr523) and
the S2′ region (His513 and His353) of ACE. Moreover, the digestion parameters were further
optimized and the target peptide (82% purity) was readily obtained (15% yield) without any
cumbersome purification procedure. Notably, lysozyme C is the most abundant protein in
SSTEW, which implies that an efficient production of this ACEI peptide from SSTEW is
promising.

期刊名稱Journal of Proteomics
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