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Constraining and Modifying Peptides Using Pd-Mediated Cysteine Allylation. | LitMetric

AI Article Synopsis

  • Researchers have developed techniques to enhance the stability and binding of peptides by inducing and stabilizing their secondary structures.
  • This study explores a new method using Pd-catalyzed cysteine allylation for creating staples in peptides, which can also be modified for additional functions like introducing probes.
  • The team tested these modifications on a specific peptide binder, LXY3, replacing disulfide bridges with staples to improve its stability and binding to integrin α β.

Article Abstract

Over the past decades, several strategies for inducing and stabilizing secondary structure formation in peptides have been developed to increase their proteolytic stability and their binding affinity to specific interaction partners. Here, we report how our recently introduced chemoselective Pd-catalyzed cysteine allylation reaction can be extended to stapling and how the resulting alkene-containing staples themselves can be further modified to introduce additional probes into such stabilized peptides. The latter is demonstrated by introducing a fluorophore as well as a PEG moiety into different stapled peptides using bioorthogonal thiol-ene and Diels-Alder reactions. Furthermore, we investigated structural implications of our allyl staples when used to replace conformationally relevant disulfide bridges. To this end, we chose a selective binder of integrin α β (LXY3), which is only active in its cyclic disulfide form. We replaced the disulfide bridge by different stapling reagents in order to increase stability and binding affinity towards integrin α β .

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC10947015PMC
http://dx.doi.org/10.1002/cbic.202300098DOI Listing

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