基质辅助激光解吸/电离质谱反映溶液相锌指肽络合情况。

Matrix-assisted laser desorption/ionization mass spectra reflect solution-phase zinc finger peptide complexation.

作者信息

Lehmann E, Zenobi R, Vetter S

机构信息

Laboratory of Organic Chemistry, ETH Zürich, Switzerland.

出版信息

J Am Soc Mass Spectrom. 1999 Jan;10(1):27-34. doi: 10.1016/S1044-0305(98)00116-0.

DOI:10.1016/S1044-0305(98)00116-0

Abstract

The complexation between an 18-residue zinc finger peptide of CCHC type (CCHC = Cys-X2-Cys-X4-His-X4-Cys, X = variable amino acid) from the gag protein p55 of human immunodeficiency virus type 1 (HIV-1) and various transition metal ions was studied by means of circular dichroism spectroscopy and matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS). A correlation between the complexation behavior in solution and in MALDI-MS could be established. It was shown that MALDI-MS is a fast method suitable for studying metal binding properties of zinc finger complexes.

摘要

利用圆二色光谱和基质辅助激光解吸/电离质谱（MALDI-MS）研究了来自人类免疫缺陷病毒1型（HIV-1）gag蛋白p55的18个残基的CCHC型锌指肽（CCHC = 半胱氨酸-X2-半胱氨酸-X4-组氨酸-X4-半胱氨酸，X = 可变氨基酸）与各种过渡金属离子之间的络合作用。可以建立溶液中络合行为与MALDI-MS中络合行为之间的相关性。结果表明，MALDI-MS是一种适用于研究锌指络合物金属结合特性的快速方法。

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