The intracellular Ig fold: a robust protein scaffold for the engineering of molecular recognition

Protein Engineering, Design & Selection : PEDS
Marc BruningOlga Mayans

Abstract

Protein scaffolds that support molecular recognition have multiple applications in biotechnology. Thus, protein frames with robust structural cores but adaptable surface loops are in continued demand. Recently, notable progress has been made in the characterization of Ig domains of intracellular origin--in particular, modular components of the titin myofilament. These Ig belong to the I(intermediate)-type, are remarkably stable, highly soluble and undemanding to produce in the cytoplasm of Escherichia coli. Using the Z1 domain from titin as representative, we show that the I-Ig fold tolerates the drastic diversification of its CD loop, constituting an effective peptide display system. We examine the stability of CD-loop-grafted Z1-peptide chimeras using differential scanning fluorimetry, Fourier transform infrared spectroscopy and nuclear magnetic resonance and demonstrate that the introduction of bioreactive affinity binders in this position does not compromise the structural integrity of the domain. Further, the binding efficiency of the exogenous peptide sequences in Z1 is analyzed using pull-down assays and isothermal titration calorimetry. We show that an internally grafted, affinity FLAG tag is functional within the conte...Continue Reading

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Citations

Jan 4, 2015·Journal of Molecular Biology·Guy M Benian, Olga Mayans
Mar 14, 2019·Advanced Materials·Christopher J HillPatricia Murray
Sep 6, 2019·International Journal of Molecular Sciences·Yevheniia NesterenkoOlga Mayans
Dec 20, 2019·PloS One·Spyros D ChatziefthimiouMatthias Wilmanns

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