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Nanomechanical in situ monitoring of proteolysis of peptide by Cathepsin B.


ABSTRACT: 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.

SUBMITTER: Kwon T 

PROVIDER: S-EPMC2707113 | biostudies-literature | 2009

REPOSITORIES: biostudies-literature

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Nanomechanical in situ monitoring of proteolysis of peptide by Cathepsin B.

Kwon Taeyun T   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  

PloS one 20090716 7


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 mas  ...[more]

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