Journal Article

Nanomechanical In Situ Monitoring of Proteolysis of Peptide by Cathepsin B

Taeyun Kwon, Chang-Wan Kim, Jin Suck Suh, Sungjoo Haam, Jaemoon Yang, Kilho Eom, Jinsung Park, Sungsoo Na, Yong Min Huh, Dae Sung Yoon

2009

Overview

Characterization and control of proteolysis of peptides by specific cellular protease is a priori requisite for effective drug discovery. Here, we report the nanomechanical, in situ monitoring of proteolysis of peptide chain attributed to protease (Cathepsin B) by using a resonant nanomechanical microcantilever immersed in a liquid. Specifically, the detection is based on measurement of resonant frequency shift arising from proteolysis of peptides (leading to decrease of cantilever's overall mass, and consequently, increases in the resonance). It is shown that resonant microcantilever enables the quantification of proteolysis efficacy with respect to protease concentration. Remarkably, the nanomechanical, in situ monitoring of proteolysis allows us to gain insight into the kinetics of proteolysis of peptides, which is well depicted by Langmuir kinetic model. This implies that nanomechanical biosensor enables the characterization of specific cellular protease such as its kinetics.

• Publisher: Public Library of Science (PLoS),Public Library of Science
• Subject: Biochemistry/Experimental Biophysical Methods / Biophysics/Experimental Biophysical Methods / Biosensors / Biotechnology/Bioengineering / Cancer / Cathepsin B / Cathepsin B - metabolism / Cathepsins / Chemistry/Biochemistry / Deoxyribonucleic acid / DNA / Drug discovery / Electrolytes / Frequency shift / Hybridization / Hydrolysis / Kinetics / Mechanical engineering / Medicine / Microscopy / Monitoring / Nanotechnology / Nanowires / Peptides / Peptides - metabolism / Polyethylene glycol / Polyethylene Glycols / Polyethylene Glycols - metabolism / Polymers / Protease / Proteinase / Proteolysis / Q / R / Research Article / RNA-protein interactions / Science