用于溶酶体半胱氨酸蛋白酶天冬酰胺内肽酶（AEP）/豆球蛋白的细胞渗透性、基于荧光活性的探针设计。
Design of cell-permeable, fluorescent activity-based probes for the lysosomal cysteine protease asparaginyl endopeptidase (AEP)/legumain.
作者信息
Sexton Kelly B, Witte Martin D, Blum Galia, Bogyo Matthew
机构信息
Department of Pathology, Stanford University School of Medicine, 300 Pasteur Dr., Stanford, CA 940305, USA.
出版信息
Bioorg Med Chem Lett. 2007 Feb 1;17(3):649-53. doi: 10.1016/j.bmcl.2006.10.100. Epub 2006 Nov 6.
Abstract
Asparaginyl endopeptidase (AEP), also known as legumain, is a cysteine protease that has been ascribed roles in antigen presentation yet its exact role in human biology remains poorly understood. We report here, the use of a positional scanning combinatorial library of peptide AOMKs containing a P1 aspartic acid to probe the P2, P3, and P4 subsite specificity of endogenous legumain. Using inhibitor specificity profiles of cathepsin B and legumain, we designed fluorescent ABPs that are highly selective, cell-permeable reagents for monitoring legumain activity in complex proteomes.
摘要
天冬酰胺内肽酶（AEP），也称为豆球蛋白，是一种半胱氨酸蛋白酶，在抗原呈递中发挥作用，但其在人类生物学中的确切作用仍知之甚少。我们在此报告，使用含有P1天冬氨酸的肽AOMK的位置扫描组合文库来探测内源性豆球蛋白的P2、P3和P4亚位点特异性。利用组织蛋白酶B和豆球蛋白的抑制剂特异性谱，我们设计了荧光ABP，它们是用于监测复杂蛋白质组中豆球蛋白活性的高选择性、细胞可渗透试剂。
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