Gyudo Lee1,2,‡, Prof. Kilho Eom1,2,‡, Joseph Park3, Prof. Jaemoon Yang1,4,*, Prof. Seungjoo Haam3, Prof. Yong-Min Huh4, Joo Kyung Ryu5, Nam Hee Kim5, Prof. Jong In Yook5, Prof. Sang Woo Lee2, Prof. Dae Sung Yoon2,*, Prof. Taeyun Kwon1,2,*
1Institute for Molecular Sciences, Seoul 120-749 (Republic of Korea)
2Department of Biomedical Engineering, Yonsei University, Wonju 220-710 (Republic of Korea)
3Department of Chemical and Biomolecular Engineering, Yonsei University, Seoul 120-749 (Republic of Korea)
4Department of Radiology, Yonsei University, Seoul 120-752 (Republic of Korea)
5Department of Oral pathology, Oral Cancer Research Institute, Yonsei University, Seoul 120-752 (Republic of Korea)
‡These authors contributed equally to this work.
*To whom correspondence may be addressed.
†This work was supported by the National Research Foundation of Korea (NRF) (under Grant No. NRF-2010-0009428, and NRF-2011-0009885).
Good vibrations: A bioassay using a resonant peptide-functionalized microcantilever enables the quantitative characterization of the proteolytic activity of membrane type-1 matrix metalloproteinase (MT1-MMP). In this assay, shifts in the frequency of the cantilever after specific proteolytic cleavage of the target peptides by MT1-MMP are measured (see picture).
Keywords:atomic force microscopy;biosensors;cancer;peptides;proteases