Read more about how to correctly acknowledge RSC content. Permission is not required) please go to the Copyright If you want to reproduce the wholeĪrticle in a third-party commercial publication (excluding your thesis/dissertation for which If you are the author of this article, you do not need to request permission to reproduce figuresĪnd diagrams provided correct acknowledgement is given. I can be as engaged as I choose to be, connecting with others at the dog park or fellow yogis in the Fitness Studio. At The Vicinity, I can thrive off the energy of a vibrant urban community yet escape and recharge in the luxury of my own home. Provided correct acknowledgement is given. This is not just my place in the Mill District, it is MY place. If you are an author contributing to an RSC publication, you do not need to request permission Please go to the Copyright Clearance Center request page. To request permission to reproduce material from this article in a commercial publication, Provided that the correct acknowledgement is given and it is not used for commercial purposes. This article in other publications, without requesting further permission from the RSC, Li,Ĭreative Commons Attribution-NonCommercial 3.0 Unported Licence. This proof-of-concept study reveals its potential for further broad biological applications.Ī sulfonium tethered peptide ligand rapidly and selectively modifies protein cysteine in vicinityĭ. This method enhances the peptide's biophysical properties and generates a selective ligand-directed reactive site for protein modification and fulfills multiple purposes by one modification. The high target specificity is further proved in cell lysate and hints at its further application in activity based protein profiling.
The conjugation reaction is rapid, facile and selective, triggered solely by proximity. Notably, when the cyclized peptide ligand selectively recognizes its protein target with a proximate cysteine, a rapid nucleophilic substitution could occur between the protein Cys and the sulfonium center on the peptide to form a conjugate. Herein, we report a unique peptide macrocyclization method via the bis-alkylation between methionine and cysteine to generate cyclic peptides with significantly enhanced stability and cellular uptake. In most cases, a reactive moiety was installed onto ligands with the sole purpose of reacting with specific residues in proteins.
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Refer to the Colour Guide for colour options, available for download in the documents section.Significant efforts have been invested to develop site-specific protein modification methodologies in the past two decades.
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