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Hinge-Type Dimerization of Proteins by a Tetracysteine Peptide of High Pairing Specificity

MPG-Autoren
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Li,  Aitao
Department of Chemistry, Philipps-Universität Marburg;
Research Department Reetz, Max-Planck-Institut für Kohlenforschung, Max Planck Society;

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Reetz,  Manfred T.
Department of Chemistry, Philipps-Universität Marburg;
Research Department Reetz, Max-Planck-Institut für Kohlenforschung, Max Planck Society;

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Zitation

Schrimpf, A., Hempel, F., Li, A., Linne, U., Maier, U. G., Reetz, M. T., et al. (2018). Hinge-Type Dimerization of Proteins by a Tetracysteine Peptide of High Pairing Specificity. Biochemistry, 57(26), 3658-3664. doi:10.1021/acs.biochem.8b00475.


Zitierlink: https://hdl.handle.net/21.11116/0000-0001-EC55-6
Zusammenfassung
Dimeric disulfide-linked peptides are formed by the regioselective oxidative folding of thiol precursors containing the CX3CX2CX3C tetracysteine motif. Here, we investigate the general applicability of this peptide as a dimerization motif for different proteins. By recombinant DNA technology, the peptide CHWECRGCRLVC was loaded with proteins, and functional homodimers were obtained upon oxidative folding. Attached to the N-terminus of the dodecapeptide, the prokaryotic enzyme limonene epoxide hydrolase (LEH) completely forms a covalent antiparallel dimer. In a diatom expression system, the monoclonal antibody CL4 mAb is released in its functional form when its natural CPPC central parallel hinge is exchanged for the designed tetra-Cys hinge motif. To improve our understanding of the regioselectivity of tetra-disulfide formation, we provoked the formation of heterodimeric hinge peptides by mixing two different tetra-Cys peptides and characterizing the heterodimer by mass spectrometry and nuclear magnetic resonance spectroscopy.