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rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
29
|
|
pubmed:dateCreated |
2009-7-22
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|
pubmed:abstractText |
It is demonstrated that sortase A (SrtA) can catalyze efficient coupling of peptides to GPI analogues with a glycine residue attached to the phosphoethanolamine moiety at the nonreducing end to form GPI-linked peptides. This represents the first chemoenzymatic synthesis of GPI-peptide conjugates and is a proof-of-concept for the potential application of SrtA to the synthesis of more complex GPI-anchored peptides/glycopeptides and GPI-anchored proteins/glycoproteins.
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pubmed:language |
eng
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pubmed:journal |
|
|
pubmed:citationSubset |
IM
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|
pubmed:chemical |
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Jul
|
|
pubmed:issn |
1520-5126
|
|
pubmed:author |
|
|
pubmed:issnType |
Electronic
|
|
pubmed:day |
29
|
|
pubmed:volume |
131
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
9878-9
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|
pubmed:meshHeading |
|
|
pubmed:year |
2009
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|
pubmed:articleTitle |
Sortase-catalyzed peptide-glycosylphosphatidylinositol analogue ligation.
|
|
pubmed:affiliation |
Department of Chemistry, Wayne State University, 5101 Cass Avenue, Detroit, Michigan 48202, USA.
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|
pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
|
