Structure and computation-guided yeast surface display for the evolution of TIMP-based matrix metalloproteinase inhibitors.

ABSTRACT: The study of protein-protein interactions (PPIs) and the engineering of protein-based inhibitors often employ two distinct strategies. One approach leverages the power of combinatorial libraries, displaying large ensembles of mutant proteins, for example, on the yeast cell surface, to select binders. Another approach harnesses computational modeling, sifting through an astronomically large number of protein sequences and attempting to predict the impact of mutations on PPI binding energy. Individually, each approach has inherent limitations, but when combined, they generate superior outcomes across diverse protein engineering endeavors. This synergistic integration of approaches aids in identifying novel binders and inhibitors, fine-tuning specificity and affinity for known binding partner

SUBMITTER: Shoari A 

PROVIDER: S-EPMC10702220 | biostudies-literature | 2023

REPOSITORIES: biostudies-literature