Nanomechanical in situ monitoring of proteolysis of peptide by Cathepsin B.
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.
Kwon
Taeyun
T
Research Institute for Engineering Technology, Korea University, Seoul, Republic of Korea. tykwon@korea.ac.kr
Park
Jinsung
J
Yang
Jaemoon
J
Yoon
Dae Sung
DS
Na
Sungsoo
S
Kim
Chang-Wan
CW
Suh
Jin-Suck
JS
Huh
Yong-Min
YM
Haam
Seungjoo
S
Eom
Kilho
K
D002401:Cathepsin B / Q000378:metabolism*; D006868:Hydrolysis; D007700:Kinetics; D036103:Nanotechnology; D010455:Peptides / Q000378:metabolism*; D011092:Polyethylene Glycols / Q000378:metabolism
D010455:Peptides; D011092:Polyethylene Glycols; D002401:Cathepsin B