Non-covalent synthesis of a multivalent enzyme

I. Baal, van, E.H.M. Lempens, J.L.J. Dongen, van, M. Merkx, E.W. Meijer

Research output: Chapter in Book/Report/Conference proceedingConference contributionAcademic

Abstract

We report the synthesis of a non-covalent protein dendrimer using the strong and highly specific interaction between S-peptide and S-protein. Assocn. of S-peptide and S-protein results in the formation of an active enzyme, RNase S, whereas neither fragment alone displays any enzyme activity. Native chem. ligation was used to couple four S-peptides via their C-terminal thioester to a cysteine-functionalized synthetic scaffold to yield a tetravalent S-peptide dendrimer. A fully functional RNase S tetramer was prepd. by addn. of four equiv. of S-protein. Complex formation was studied using a fluorescent enzyme activity assay and mass spectrometry. This new strategy towards multivalent proteins can be used to synthesize complex semi-synthetic protein assemblies, which may find applications in nanomedicine or functional biomaterials. [on SciFinder (R)]
Original languageEnglish
Title of host publicationProceedings of the 233rd ACS National Meeting, March 25-29, 2007, Chicago, IL, United States
PagesMSE-473
Publication statusPublished - 2007

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