Exploring the Thermostability of CRISPR-Cas12b using Molecular Dynamics Simulations.

ABSTRACT: CRISPR (clustered regularly interspaced short palindromic repeat)-based diagnostics are at the forefront of rapid detection platforms of infectious diseases. The integration of reverse transcription-loop-mediated isothermal amplification (RT-LAMP) with CRISPR-Cas protein systems has led to the creation of advanced one-pot assays. The sensitivity of these assays has been bolstered by the utilization of a thermophilic Cas12 protein, BrCas12b, and its engineered variant, which exhibits enhanced thermal stability and allows for broader operation temperatures of the assay. Here, we perform all-atom molecular dynamics (MD) simulations on wild-type and mutant BrCas12b to reveal the mechanism of stabilization conferred by the mutation. High-temperature simulations reveal a small structural change

SUBMITTER: Jia Y 

PROVIDER: S-EPMC11383325 | biostudies-literature | 2024 Aug

REPOSITORIES: biostudies-literature