DisruPPI: structure-based computational redesign algorithm for protein binding disruption.

ABSTRACT:

Motivation

Disruption of protein-protein interactions can mitigate antibody recognition of therapeutic proteins, yield monomeric forms of oligomeric proteins, and elucidate signaling mechanisms, among other applications. While designing affinity-enhancing mutations remains generally quite challenging, both statistically and physically based computational methods can precisely identify affinity-reducing mutations. In order to leverage this ability to design variants of a target protein with disrupted interactions, we developed the DisruPPI protein design method (DISRUpting Protein-Protein Interactions) to optimize combinations of mutations simultaneously for both disruption and stability, so that incorporated disruptive mutations do not inadvertently affect the target protein advers

SUBMITTER: Choi Y 

PROVIDER: S-EPMC6022686 | biostudies-literature | 2018 Jul

REPOSITORIES: biostudies-literature