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- W2743290605 endingPage "5030" @default.
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- W2743290605 abstract "Protein-templated reactions have been used for fragment-based drug discovery as well as for covalent labeling, detection and manipulation of proteins. In spite of the growing interest in protein-templated reactions, little is known about the design criteria. Herein we present a systematic study on the effects of proximity in peptide-templated reactions. To facilitate reaction monitoring at low concentrations we developed a fluorogenic native chemical ligation that is based on the integration of a fluorescence quencher in the thiol leaving group. The reaction system provided up to 39-fold increases of emission from a fluorescein unit. By using templates based on coiled coils as models we investigated the effect of misalignments. The distance-reactivity pattern for remotely aligned peptides was remarkably different to reaction scenarios that involved seamlessly annealed peptides with overhanging functional groups." @default.
- W2743290605 created "2017-08-17" @default.
- W2743290605 creator A5043944404 @default.
- W2743290605 creator A5083922106 @default.
- W2743290605 date "2017-09-01" @default.
- W2743290605 modified "2023-10-09" @default.
- W2743290605 title "A fluorogenic native chemical ligation for assessing the role of distance in peptide-templated peptide ligation" @default.
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- W2743290605 doi "https://doi.org/10.1016/j.bmc.2017.08.007" @default.
- W2743290605 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/28823838" @default.
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