Document Detail


Synthesis of tetrapeptide p-nitrophenylanilides containing dehydroalanine and dehydrophenylalanine and their influence on cathepsin C activity.
MedLine Citation:
PMID:  11297349     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Three dehydrotetrapeptides of rationally varying structure were prepared and tested as affectors of cathepsin C. These compounds appeared to be substrates of the enzyme, being equipotent with their classical counterparts. Thus, replacement of amino acid in a short peptide by corresponding dehydroamino acid does not prevent cathepsin C in recognizing dehydropeptide as its substrate.
Authors:
M Makowski; M Pawelczak; R Latajka; K Nowak; P Kafarski
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Journal of peptide science : an official publication of the European Peptide Society     Volume:  7     ISSN:  1075-2617     ISO Abbreviation:  J. Pept. Sci.     Publication Date:  2001 Mar 
Date Detail:
Created Date:  2001-04-11     Completed Date:  2001-07-26     Revised Date:  2009-11-19    
Medline Journal Info:
Nlm Unique ID:  9506309     Medline TA:  J Pept Sci     Country:  England    
Other Details:
Languages:  eng     Pagination:  141-5     Citation Subset:  IM    
Affiliation:
Institute of Chemistry, University of Opole, Oleska, Poland.
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MeSH Terms
Descriptor/Qualifier:
Alanine / analogs & derivatives*,  chemistry*
Amino Acids / chemistry
Anilides / chemical synthesis*,  chemistry
Animals
Cathepsin C / chemistry,  metabolism*
Cattle
Magnetic Resonance Spectroscopy
Models, Chemical
Oligopeptides / chemical synthesis*,  chemistry
Phenylalanine / analogs & derivatives*,  chemistry*
Spleen / metabolism
Chemical
Reg. No./Substance:
0/Amino Acids; 0/Anilides; 0/Oligopeptides; 1948-56-7/dehydroalanine; 56-41-7/Alanine; 63-91-2/Phenylalanine; 7060-39-1/phenyldehydroalanine; EC 3.4.14.1/Cathepsin C

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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