带羟乙基侧臂三脚架多胺Cu(Ⅱ)配合物切割肌红蛋白所得片断的质谱指认(英文)

Mass Spectrometry Assisted Assignments of Fragments of Myoglobin Cleaved by Copper(II) Complex with Tripodal Polyamimine Bearing an Hydroxyethyl Pendant

采用电喷雾质谱和串联质谱以及聚丙烯酰胺凝胶电泳技术研究了[CuL(H2O)](BF4)2(L为2-[二(2-氨乙酸)氨基]乙醇)与马心肌红蛋白的键合作用和水解切割。聚丙烯酰胺凝胶电泳研究显示在中性及60℃条件下,切割效率与[CuL(H2O)]2+的浓度和温育时间密切相关。电喷雾质谱和串联质谱分析显示,[CuL(H2O)]2+通过与肌红蛋白的氨基酸His36,His93,His116和Arg139侧链的结合,并在羟乙基侧臂的促进下,选择性地水解了肽键Phe33-Thr34,Gln91-Ser92,Ala94-Thr95,His116-Ser117和Asn140-Asp141。

The bonding interaction and hydrolytic cleavage of horse heart myoglobin with [CuL（H2O）]（BF4）2, where L is 2-[bis （2-aminoethyl）amino]ethanol, were investigated by electrospray ionization mass spectrometry（ESI-MS）, tandem mass spectrometry （MS/MS） and SDS-PAGE electrophoresis. The SDS-PAGE electrophoresis showed that the cleavage yield was dependent on the concentration of [CuL（H2O）]^2＋ and incubation time. The ESI-MS and MS/MS analysis revealed that with the assistance of the pendant hydroxyl group in [CuL（H2O）]^2＋, [CuL（H2O）]^2＋ may selectively hydrolysis the peptide bonds of Phe33-Thr34, Gln91-Ser92, Ala94-Thr95, His116-Ser117 and Asn140- Asp141 of myoglobin by the binding of [CuL（H2O）]^2＋ to the side chains of His36, His93, His116 and Arg139 of myoglobin.