Dresden 2017 – scientific programme

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CPP: Fachverband Chemische Physik und Polymerphysik

CPP 45: Biomaterials and Biopolymers (joint session BP/CPP, organized by BP)

CPP 45.8: Talk

Wednesday, March 22, 2017, 17:00–17:15, SCH A251

Tuning coiled coils mechanically and thermodynamically by histidine-metal coordination — •Isabell Tunn, Kerstin G. Blank, and Matthew J. Harrington — Max Planck Institute of Colloids and Interfaces, Science Park Potsdam Golm, 14424 Potsdam

Coiled coils serve as structural motifs in proteins with mechanical function, such as myosin or α-keratin. In the field of bioinspired materials, naturally occurring and synthetic coiled coils with high binding specificity have become versatile material building blocks, which are used as crosslinkers for hydrogels with applications in cell culture and tissue engineering. Very little is currently understood about the mechanical properties of coiled coils. Yet, this information is critical for controlling and tuning bulk properties of coiled coil-based materials. In order to generate mechanically tunable coiled-coil based materials, metal coordination sites were engineered into a well-characterized heterodimeric coiled coil. Protein-metal coordination bonds are strong, non-covalent interactions mediated by amino acid ligands. Here, two histidine residues were introduced at the coiled coil termini with the goal of stabilizing helical turns. Histidine-metal coordination increased the stability of the coiled coil mechanically and thermodynamically, as demonstrated by AFM single molecule force spectroscopy and CD spectroscopy. We conclude that increasing the stability of single helical turns via metal binding directly affects the overall stability of the coiled coil, providing the potential for generating mechanically tunable biomimetic polymers. Furthermore, these results also provide crucial information about the failure mechanism of coiled coils under load.