title: Stability of synthetic exendin-4 in human plasma in vitro.
abstract: Sites of exendin-4 that that are relatively susceptible to degradation in plasma were identified with the aim of providing information for designing new exendin-4 analogues. The stability of exendin-4 in human plasma was evaluated in vitro. The results showed that the peptide was slowly degraded with a half-life of 9.57 h and the principal cleavage sites are between Thr5 and Phe6, Phe6 and Thr7, and Thr7 and Ser8 of the N-terminus region of exendin-4.
authors.affiliation: College of Life Science, Jilin University, Changchun 130012, P.R. China.
authors.forename: Jie
authors.initials: J
authors.lastname: Chen
authors.forename: Ling
authors.initials: L
authors.lastname: Yu
authors.forename: Liping
authors.initials: L
authors.lastname: Wang
authors.forename: Xuexun
authors.initials: X
authors.lastname: Fang
authors.forename: Li
authors.initials: L
authors.lastname: Li
authors.forename: Wei
authors.initials: W
authors.lastname: Li
mesh_terms: D000595:Amino Acid Sequence; D002851:Chromatography, High Pressure Liquid; D000077270:Exenatide; D052216:Glucagon-Like Peptide 1 / Q000737:chemistry; D006801:Humans; D008969:Molecular Sequence Data; D010455:Peptides / Q000097:blood* / Q000737:chemistry*; D017433:Protein Structure, Secondary; D014688:Venoms / Q000097:blood* / Q000737:chemistry*
chemical_list: D010455:Peptides; D014688:Venoms; D052216:Glucagon-Like Peptide 1; D000077270:Exenatide