Selective, non-covalent conjugation of synthetic peptides with recombinant proteins mediated by host-guest chemistry.
Loading...
Date
Journal Title
Journal ISSN
Volume Title
Publisher
Royal Society of Chemistry (RSC)
https://doi.org/10.1039/c6cc00405a
https://doi.org/10.1039/c6cc00405a
Abstract
Description
The combination of potent chemical moieties with biologically active proteins is key to some of today's most innovative therapeutic drugs. In order to obviate any chemical modification of the proteins, we present a novel and powerful strategy for the selective conjugation of recombinant protein domains with synthetically derived peptides via a cucurbit[8]uril host-guest chemistry approach.
We thank Alexandra Rieck, Isabelle Sermadiras, Benjamin Kemp and Jennifer Spooner for help with the expression and purification of the Fc and Tn3 domains, Jefferson Revell and Jacky Metcalfe for help with the synthesis of modified peptides and Christel Veyssier for help with the light scattering experiments. RJG was supported by the MedImmune postdoctoral program. SS was supported by ERC Starting Investigator grant ASPiRe (No. 240629).
This is the final version of the article. It first appeared from Royal Society of Chemistry via http://dx.doi.org/10.1039/C6CC00405A
We thank Alexandra Rieck, Isabelle Sermadiras, Benjamin Kemp and Jennifer Spooner for help with the expression and purification of the Fc and Tn3 domains, Jefferson Revell and Jacky Metcalfe for help with the synthesis of modified peptides and Christel Veyssier for help with the light scattering experiments. RJG was supported by the MedImmune postdoctoral program. SS was supported by ERC Starting Investigator grant ASPiRe (No. 240629).
This is the final version of the article. It first appeared from Royal Society of Chemistry via http://dx.doi.org/10.1039/C6CC00405A