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http://purl.uniprot.org/citations/27596722http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/27596722http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/27596722http://www.w3.org/2000/01/rdf-schema#comment"Macrocyclization can be used to constrain peptides in their bioactive conformations, thereby supporting target affinity and bioactivity. In particular, for the targeting of challenging protein-protein interactions, macrocyclic peptides have proven to be very useful. Available approaches focus on the stabilization of α-helices, which limits their general applicability. Here we report for the first time on the use of ring-closing alkyne metathesis for the stabilization of an irregular peptide secondary structure. A small library of alkyne-crosslinked peptides provided a number of derivatives with improved target affinity relative to the linear parent peptide. In addition, we report the crystal structure of the highest-affinity derivative in a complex with its protein target 14-3-3ζ. It can be expected that the alkyne-based macrocyclization of irregular binding epitopes should give rise to new scaffolds suitable for targeting of currently intractable proteins."xsd:string
http://purl.uniprot.org/citations/27596722http://purl.org/dc/terms/identifier"doi:10.1002/cbic.201600362"xsd:string
http://purl.uniprot.org/citations/27596722http://purl.org/dc/terms/identifier"doi:10.1002/cbic.201600362"xsd:string
http://purl.uniprot.org/citations/27596722http://purl.uniprot.org/core/author"Ottmann C."xsd:string
http://purl.uniprot.org/citations/27596722http://purl.uniprot.org/core/author"Ottmann C."xsd:string
http://purl.uniprot.org/citations/27596722http://purl.uniprot.org/core/author"Grossmann T.N."xsd:string
http://purl.uniprot.org/citations/27596722http://purl.uniprot.org/core/author"Grossmann T.N."xsd:string
http://purl.uniprot.org/citations/27596722http://purl.uniprot.org/core/author"Glas A."xsd:string
http://purl.uniprot.org/citations/27596722http://purl.uniprot.org/core/author"Glas A."xsd:string
http://purl.uniprot.org/citations/27596722http://purl.uniprot.org/core/author"Bier D."xsd:string
http://purl.uniprot.org/citations/27596722http://purl.uniprot.org/core/author"Bier D."xsd:string
http://purl.uniprot.org/citations/27596722http://purl.uniprot.org/core/author"Cromm P.M."xsd:string
http://purl.uniprot.org/citations/27596722http://purl.uniprot.org/core/author"Cromm P.M."xsd:string
http://purl.uniprot.org/citations/27596722http://purl.uniprot.org/core/author"Furstner A."xsd:string
http://purl.uniprot.org/citations/27596722http://purl.uniprot.org/core/author"Furstner A."xsd:string
http://purl.uniprot.org/citations/27596722http://purl.uniprot.org/core/author"Wallraven K."xsd:string
http://purl.uniprot.org/citations/27596722http://purl.uniprot.org/core/author"Wallraven K."xsd:string
http://purl.uniprot.org/citations/27596722http://purl.uniprot.org/core/date"2016"xsd:gYear
http://purl.uniprot.org/citations/27596722http://purl.uniprot.org/core/date"2016"xsd:gYear
http://purl.uniprot.org/citations/27596722http://purl.uniprot.org/core/name"ChemBioChem"xsd:string
http://purl.uniprot.org/citations/27596722http://purl.uniprot.org/core/name"Chembiochem"xsd:string
http://purl.uniprot.org/citations/27596722http://purl.uniprot.org/core/pages"1915-1919"xsd:string
http://purl.uniprot.org/citations/27596722http://purl.uniprot.org/core/pages"1915-1919"xsd:string