Structural Bases for Chemical and Mechanical Gating in the Piezo1 Channel

Abstract

various peptide concentrations and pH levels. The absorbance transitions are sensitive to the formation of the electronically conductive J-aggregate, allowing for rapid spectroscopic identification. Fluorescence spectroscopy, circular dichroism, and dynamic light scattering were also used to assess J-aggregate formation. The peptides were shown to induce the formation of J-aggregates up to solution pH 3.0, but maintains the ability to bind porphyrin at neutral pH. Notably, the peptides were shown to adopt an unstructured conformation at low pH but become somewhat helical at neutral pH. Studies of mixed peptide binding stoichiometry indicate formation of complementary heterooligomers that retain their porphyrin-binding capabilities and produce an additional binding site at their junction. These results have implications for the design of photoelectronically active biomaterials. 2366-PosOptimization of the Site-Identification by Ligand Competitive Saturation (SILCS) as an Accurate and Reliable Technique in Lead Optimization