Using peptidyl aldehydes in activity-based proteomics

被引：6

作者：

Sabido, Eduard ^{[1
,2
]}

Tarrago, Teresa ^{[2
]}

Giralt, Ernest ^{[1
,2
]}

机构：

[1] Univ Barcelona, Dept Quim Organ, E-08028 Barcelona, Spain

[2] Inst Recerca Biomed, Barcelona 08028, Spain

来源：

BIOORGANIC & MEDICINAL CHEMISTRY LETTERS | 2009年 / 19卷 / 14期

关键词：

Aldehydes; Peptides; Activity-based proteomics; Prolyl oligopeptidase; PROLYL ENDOPEPTIDASE INHIBITOR; ACTIVITY-BASED PROBES; REVERSIBLE COVALENT INHIBITORS; PROTEIN-TYROSINE PHOSPHATASES; SERINE HYDROLASE ACTIVITIES; SOLID-PHASE; ARGININE-VASOPRESSIN; SELECTIVE INHIBITORS; CHEMICAL PROTEOMICS; CYSTEINE PROTEASES;

D O I：

10.1016/j.bmcl.2009.04.148

中图分类号：

R914 [药物化学];

学科分类号：

100701 ;

摘要：

The broad inhibitory spectrum of aldehydes and the possibility that amino acid residues modulate their specificity point to the potential of using peptidyl aldehydes as activity-based probes. Here, we establish the potential of peptidyl aldehydes in activity-based proteomics by synthesizing different probes and using them to specifically label a well-known serine protease in an activity-dependent manner. From our results, peptidyl aldehydes emerge as promising activity-based probes that enable multiple enzymatic-class detection by substrate recognition and can be used in diverse activity-based proteomics applications like protein identification and activity profiling. (C) 2009 Elsevier Ltd. All rights reserved.

引用

页码：3752 / 3755

页数：4

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