These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: Synthesis and evaluation of new elastase substrates as tripartate prodrugs.
    Author: Achilles K.
    Journal: Arch Pharm (Weinheim); 2002 Jul; 335(7):325-30. PubMed ID: 12207282.
    Abstract:
    Compounds consisting of a peptide sequence, 4-aminobutyric acid or 5-aminovaleric acid, respectively, as spacer units, and benzyl alcohol as a model leaving group have been prepared and tested for their ability to serve as substrates for porcine pancreatic elastase and human polymorphnuclear elastase. Those compounds containing an Ala-Ala-Ala sequence served as effective substrates for both enzymes. Hydrolytic cleavage, however, occurred exclusively at the ester bond, not at the peptide-spacer bond. In order to direct the cleavage site from the ester to the amide bond the peptide sequence was varied. We introduced a proline residue in P(3) (in relation to the ester bond) which is known to prevent the cleavage of a substrate by elastase. No hydrolysis, however, either of the ester bond or of the peptide-spacer bond, was found for these compounds.
    [Abstract] [Full Text] [Related] [New Search]