PROJECT #18432 RESEARCH FOR UNSPECIFIED
FOLDING PERFORMANCE PROFILE

PROJECT SUMMARY

Biofilms are aggregations of bacteria that occur in response to external stresses.  They are found in natural, industrial, and clinical environments, where they can be an impediment to effective antibiotic treatments.  In Pseudomonas fluorescens, this process is initiated by the Lap system, particularly the LapA adhesin. LapG, a periplasmic protease, cleaves the N-terminus of LapA, releasing it from its adherent surface and inhibiting the ability to form a biofilm. LapG’s ability to cleave LapA is prevented by LapD, which keeps the protease away from the cell surface through a unique protein-protein interaction (PPI) interface involving a highly conserved tryptophan of LapD.

In an effort to develop molecules that can disrupt biofilm formation, the Bahl lab at the Institute for Protein Innovation has de novo designed high-affinity mini-proteins that mimic LapD and bind LapG.  In this collaborative project, the Voelz lab is using ab initio binding simulations of these mini-proteins to understand the binding mechanism, and investigate how sequence variability influences the binding reaction.

PROJECT INFO

Manager(s): Prof. Vincent Voelz

Institution: Temple University

PROJECT WORK UNIT SUMMARY

Atoms: 60,340

Core: OPENMM_22

Status: Public