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Optimizing nanotool structure for tracking proteins

June 2018. Detailed observations of the dynamics and interactions of proteins in cells is essential for a more system-based understanding of biological processes and their dysregulation in disease. More refined tools are needed to improve the tracing of proteins at a high spatiotemporal resolution. A team of scientists from the Institute of Biochemistry at Goethe University Frankfurt have published a study on the refinement of an important type of nanotool which will open up new perspectives for ultra-small, non-disturbing and high-affinity labelling to gain deeper insights into dynamic cellular structures and processes.

Small chemical/biological interaction pairs are at the forefront in tracing protein function and interaction at a high signal‐to‐background ratio in cellular pathways. Scientists from the Institute of Biochemistry at Goethe-University Frankfurt conducted a systematic investigation into the optimal design of a specific type of these nanotools. The metal chelating N-nitrilotriacetic acid (NTA) and the oligohistidine-tag (His-tag) constitute a well-established interaction pair. So far, the His-tag is the smallest and most commonly used affinity tag in life sciences, making it an attractive target for site-specific protein labeling and in vitro or in vivo screening approaches. The scientists assembled a library of NTA-based multivalent chelator heads (MCHs) built up on linear, cyclic, and dendritic scaffolds, and compared their binding affinity and stability for the labelling of cellular His‐tagged proteins. The team observed that substantial differences exist between cyclic, linear and dendritic MCHs, underlining that the structural organization of the NTA elements is important for high affinity and kinetic stability. The scientists describe the fine-tuned optimization of trivalent chelator heads towards the highest affinity (i.e. lower probe concentration), kinetic stability and specificity (lower background) and report which of the currently available MCH probes are best suited for applications in the life sciences. More...

Contact:
Robert Tampé, Institute of Biochemistry, Faculty of Biochemistry, Chemistry and Pharmacy, Riedberg Campus, Goethe University, Frankfurt/Main, Germany, Tel.: +49(0)69-798-29475, tampe@em.uni-frankfurt.de

Publication:
Gatterdam K, Joest EF, Gatterdam V, Tampé R (2018) Scaffold design of trivalent chelator heads dictates high-affinity and stable His-tagged protein labeling in vitro and in cellulo. Angewandte Chemie - International Edition: published online 29 May 2018. http://dx.doi.org/10.1002/anie.201802746