Chan Cao

This study demonstrates the ability to detect and discriminate microcystin congeners at sub-nanomolar concentrations using aerolysin nanopores, with applications for environmental monitoring.

This study screens antimicrobial peptides using a mechanism-driven approach, identifying seven peptides with membrane-targeting and pore-forming activity that show antimicrobial efficacy with low cytotoxicity.

The paper explores new nanopore sensors from the aerolysin family by analyzing structure and sensing capabilities of three family members, finding ETX can translocate ssDNA with higher sensitivity than aerolysin.

The paper presents high-resolution cryo-EM structures of aerolysin pre-pore and pore in a membrane-like environment, revealing key interactions and constriction rings relevant for nanopore sensing.

This paper demonstrates the use of an aerolysin nanopore to identify unlabeled full-length proteins through charge-based fingerprinting, achieving 80% accuracy in distinguishing related proteins.

This study uses AR-SHS and current measurements to analyze aerolysin's membrane association and pore formation at femtomolar concentrations, revealing binding affinities and structural changes during the process.

This study uses single-molecule nanopore experiments to demonstrate Hsp70 chaperones exert forces equivalent to 46 pN to extract trapped polypeptides, supporting the Entropic Pulling mechanism.

This study uses a biological nanopore and deep learning to detect and distinguish single and multiple PTMs on -synuclein peptides at picomolar concentrations.