Linked Life Data

19377969

Source:http://linkedlifedata.com/resource/pubmed/id/19377969

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
2009-4-20
pubmed:abstractText
All proteases and peptidases are to some extent sequence-specific, in that one or more residues are preferred at particular positions surrounding the cleavage site in substrates. I describe here a general protocol for determining protease cleavage site preferences using mixture-based peptide libraries. Initially a completely random, amino-terminally capped peptide mixture is digested with the protease of interest, and the cleavage products are analyzed by automated Edman sequencing. The distribution of amino acids found in each sequencing cycle indicates which residues are preferred by the protease at positions downstream of the cleavage site. On the basis of these results, a second peptide library is designed that is partially degenerate and partially fixed sequence. Edman sequencing analysis of the cleavage products of this peptide mixture provides preferences amino-terminal to the scissile bond. As necessary, the process is reiterated until the full cleavage motif of the protease is known. Cleavage specificity data obtained with this method have been used to generate specific and efficient peptide substrates, to design potent and specific inhibitors, and to identify novel protease substrates.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
1064-3745
pubmed:author
pubmed:issnType
Print
pubmed:volume
539
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
79-91
pubmed:meshHeading
pubmed:year
2009
pubmed:articleTitle
Mixture-based peptide libraries for identifying protease cleavage motifs.
pubmed:affiliation
Department of Pharmacology, Yale University School of Medicine, New Haven, CT, USA.
pubmed:publicationType
Journal Article