Earticle

초록

영어

Among proteases, matrix metalloproteinases (MMPs) have been of significant interest because they are considered as one of promising biomarkers in association with cancer metastasis, inflammation and other degenerative diseases. Many attempts based on the optical sensing have been made to analyze the activity of MMPs, but most of them require an expensive fluorescent readout and a labor-intensive process. To circumvent this issue, we demonstrate here gold nanoparticle (AuNP)-based colorimetric assay which allows MMP activity to be monitored in a simple and rapid way. This approach is based on the self-aggregation of AuNPs through the coordination effect between the carboxyl groups of AuNPs and hexahistidine at both ends of peptide substrates in the presence of divalent metal ions. The AuNPs were easily aggregated and changed in color (from brown-red to violet) after adding the peptide substrates and metal ions without MMPs, whereas the presence of MMPs in solution prevented the NP aggregation by cleaving the peptide, thus retaining the original color of the AuNPs. Based on this principle, we analyzed the MMP activity in terms of metal ion species, buffer strength, assaying time, and MMP concentration. Given the specificity of targeting MMPs by controlling the peptide substrate, this approach is anticipated to dissect the physiological roles of many MMPs from complex biological media in a high-throughput manner.

키워드

저자

• Gae Baik KIM [ Dept. of Life Science, Hanyang University, Seoul, 133-791. ]
• Kun Hee KIM [ Dept. of Bioengineering, Hanyang University, Seoul, 133-791. ]
• Yeon Hee PARK [ Dept. of Bioengineering, Hanyang University, Seoul, 133-791. ]
• Young-Pil KIM [ Dept. of Life Science, Hanyang University, Seoul, 133-791. ]

참고문헌

발행기관

간행물

표지보기 관심저널 등록

• 간행물명

  한국생물공학회 학술대회

• 간기

  반년간

• 수록기간

  1985~2013

• 십진분류

  KDC 476 DDC 576