Manuel Isaias Osorio Soto

TITLE:

Protein Evolution for Biomimetic Biomineralization and Material Synthesis

ABSTRACT:

The functional versatility of proteins enables their rational redesign through directed evolution for applications in materials science. Techniques such as high-throughput mutant screening facilitate enzyme optimization, enhancing catalytic kinetics or modifying substrate specificity—including metal-binding capabilities beyond native function[1][2]. By employing molecular dynamics simulations and free energy calculations, it is possible to engineer mutant proteins with enhanced target affinity. Similarly, structural proteins like recombinant spider silk can be adapted for integration into flexible electronics. This approach is augmented by in silico simulation tools, which accelerate the de novo design of proteins with customized functionalities. In nature, biomineralization—orchestrated by proteins such as collagen, osteopontin, and N16—provides a blueprint for fabricating advanced composite materials[3]. A prominent example is osteocalcin, which exhibits promiscuous binding to various bivalent metals beyond calcium, suggesting its potential for in vitro evolution to direct nucleation of non-biological minerals[4]. This structural plasticity positions osteocalcin as a promising template for designing hybrid materials by leveraging its affinity for diverse metal cations. The convergence of biomimetic biomineralization and protein evolution enables sustainable design of tailored materials with programmable properties. References [1]Packer, Michael S., and David R. Liu. “Methods for the directed evolution of proteins.” Nature Reviews Genetics 16.7 (2015): 379-394. [2]Osorio, Manuel I., et al. “Structural factors that determine the activity of the xenobiotic reductase B enzyme from pseudomonas putida on nitroaromatic compounds.” International Journal of Molecular Sciences 24.1 (2022): 400. [3]Giachelli, Cecilia M., and Susan Steitz. “Osteopontin: a versatile regulator of inflammation and biomineralization.” Matrix Biology 19.7 (2000): 615-622. [4]Nousiainen, Marjaana, et al. “A mass spectrometric study of metal binding to osteocalcin.” Chemistry & biology 9.2 (2002): 195-202.