Journal
ANALYTICAL BIOCHEMISTRY
Volume 466, Issue -, Pages 30-37Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.ab.2014.08.010
Keywords
Cathepsin L; FRET peptides; Fluorescent assay; Cancer
Funding
- National Science Centre (NCN) in Poland [UMO-2012/07/N/ST5/00128]
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Internally quenched cathepsin L (Cat L) substrate ABZ-Bip-Arg-Ala-Gln-Tyr(3-NO2)-NH2 with high specificity constant (k(cat)/K-M = 2.6 x 10(7) M-1 s(-1)) was synthesized. The resultant compound displayed high selectivity over other members of the cathepsin family (B, S, X, V, C, K, H, F, D, and A). Activity of Cat L at picomolar (pM) concentrations was found using this substrate. Moreover, it was established that the presence of the selective Cat L inhibitor suppressed the proteolysis of the substrate to a non-detectable level. Incubation of the synthesized compound with a cell lysate of healthy and cancer cell lines indicated significant differences in Cat L activity. Based on the obtained results, it is proposed that this substrate could be used for selective monitoring of Cat L activity in biological systems. (C) 2014 Elsevier Inc. All rights reserved.
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