Unnatural amino acids increase activity and specificity of synthetic substrates for human and malarial cathepsin C

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• 作者：Marcin Poreba (1)
  Marko Mihelic (2)
  Priscilla Krai (3)
  Jelena Rajkovic (2)
  Artur Krezel (4)
  Malgorzata Pawelczak (5)
  Michael Klemba (3)
  Dusan Turk (2)
  Boris Turk (2)
  Rafal Latajka (1)
  Marcin Drag (1)
  
• 关键词：Cysteine protease ; Non ; proteinogenic ; Unnatural amino acid ; Substrate library ; Fluorogenic substrate
• 刊名：Amino Acids
• 出版年：2014
• 出版时间：April 2014
• 年：2014
• 卷：46
• 期：4
• 页码：931-943
• 全文大小：1,230 KB
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• 作者单位：Marcin Poreba (1)
  Marko Mihelic (2)
  Priscilla Krai (3)
  Jelena Rajkovic (2)
  Artur Krezel (4)
  Malgorzata Pawelczak (5)
  Michael Klemba (3)
  Dusan Turk (2)
  Boris Turk (2)
  Rafal Latajka (1)
  Marcin Drag (1)
  
  1. Division of Bioorganic Chemistry, Faculty of Chemistry, Wroclaw University of Technology, Wybrzeze Wyspianskiego 27, 50-370, Wroc艂aw, Poland
  2. Department of Biochemistry and Molecular and Structural Biology, Jozef Stefan Institute, Ljubljana, Slovenia
  3. Department of Biochemistry, Virginia Tech, Blacksburg, VA, 24061, USA
  4. Laboratory of Chemical Biology, Faculty of Biotechnology, University of Wroc艂aw, ul. Joliot-Curie 14a, 50-383, Wroc艂aw, Poland
  5. Faculty of Chemistry, University of Opole, ul. Oleska 48, 45-052, Opole, Poland
  
• ISSN：1438-2199

文摘

Mammalian cathepsin C is primarily responsible for the removal of N-terminal dipeptides and activation of several serine proteases in inflammatory or immune cells, while its malarial parasite ortholog dipeptidyl aminopeptidase 1 plays a crucial role in catabolizing the hemoglobin of its host erythrocyte. In this report, we describe the systematic substrate specificity analysis of three cathepsin C orthologs from Homo sapiens (human), Bos taurus (bovine) and Plasmodium falciparum (malaria parasite). Here, we present a new approach with a tailored fluorogenic substrate library designed and synthesized to probe the S1 and S2 pocket preferences of these enzymes with both natural and a broad range of unnatural amino acids. Our approach identified very efficiently hydrolyzed substrates containing unnatural amino acids, which resulted in the design of significantly better substrates than those previously known. Additionally, in this study significant differences in terms of the structures of optimal substrates for human and malarial orthologs are important from the therapeutic point of view. These data can be also used for the design of specific inhibitors or activity-based probes.