二硒醚
硒代半胱氨酸
圆二色性
半胱氨酸
化学
肽
表皮生长因子
二硫键
残留物(化学)
立体化学
生物化学
硒
有机化学
酶
受体
作者
Toshiki Takei,Hideaki Tanaka,Nobuaki Okumura,Toshifumi Takao,Luis Moröder,Hironobu Hojo
摘要
Human seleno-epidermal growth factor (seleno-EGF), a 53-residue peptide where all six cysteine residues of the parent human EGF sequence were replaced by selenocysteines, was synthesized and the oxidative folding of a polypeptide containing three diselenide bonds was compared to that of the parent cysteine peptide. The crude high performance liquid chromatography (HPLC) profiles clearly showed that both the native EGF and its selenocysteine-analogue fold smoothly, yielding a single sharp peak, proving that even in the case of three disulfide-bonded polypeptides the disulfide-to-diselenide bond substitution is highly isomorphous, as confirmed by conformational circular dichroism measurements and particularly by the biological assays.
科研通智能强力驱动
Strongly Powered by AbleSci AI