Next Article in Journal
Synthesis of New Series of 2-C-(β-D-glucopyranosyl)-Pyrimidines and Their Evaluation as Inhibitors of Some Glycoenzymes
Previous Article in Journal
Thermodynamic Driving Forces and Chemical Reaction Fluxes; Reflections on the Steady State
Review

A Review of Small Molecule Inhibitors and Functional Probes of Human Cathepsin L

by 1,2,*,† and 1,2,*
1
Chemistry and Biochemistry Department, Queens College of The City University of New York, 65-30 Kissena Blvd, Flushing, NY 11367, USA
2
Ph.D. Program in Biochemistry, The Graduate Center of the City University of New York (CUNY), 365 5th Ave, New York, NY 10016, USA
*
Authors to whom correspondence should be addressed.
Current Address: KemPharm Inc., 2200 Kraft Drive, Blacksburg, VA 24060, USA.
Molecules 2020, 25(3), 698; https://doi.org/10.3390/molecules25030698
Received: 16 December 2019 / Revised: 29 January 2020 / Accepted: 4 February 2020 / Published: 6 February 2020
(This article belongs to the Section Chemical Biology)
Human cathepsin L belongs to the cathepsin family of proteolytic enzymes with primarily an endopeptidase activity. Although its primary functions were originally thought to be only of a housekeeping enzyme that degraded intracellular and endocytosed proteins in lysosome, numerous recent studies suggest that it plays many critical and specific roles in diverse cellular settings. Not surprisingly, the dysregulated function of cathepsin L has manifested itself in several human diseases, making it an attractive target for drug development. Unfortunately, several redundant and isoform-specific functions have recently emerged, adding complexities to the drug discovery process. To address this, a series of chemical biology tools have been developed that helped define cathepsin L biology with exquisite precision in specific cellular contexts. This review elaborates on the recently developed small molecule inhibitors and probes of human cathepsin L, outlining their mechanisms of action, and describing their potential utilities in dissecting unknown function. View Full-Text
Keywords: human cathepsin L; cathepsin L probe; cathepsin L inhibitor; activity-based probes; clickable ABP; E-64; CA-074; KDP-1; cathepsin L ABP human cathepsin L; cathepsin L probe; cathepsin L inhibitor; activity-based probes; clickable ABP; E-64; CA-074; KDP-1; cathepsin L ABP
Show Figures

Figure 1

MDPI and ACS Style

Dana, D.; Pathak, S.K. A Review of Small Molecule Inhibitors and Functional Probes of Human Cathepsin L. Molecules 2020, 25, 698. https://doi.org/10.3390/molecules25030698

AMA Style

Dana D, Pathak SK. A Review of Small Molecule Inhibitors and Functional Probes of Human Cathepsin L. Molecules. 2020; 25(3):698. https://doi.org/10.3390/molecules25030698

Chicago/Turabian Style

Dana, Dibyendu; Pathak, Sanjai K. 2020. "A Review of Small Molecule Inhibitors and Functional Probes of Human Cathepsin L" Molecules 25, no. 3: 698. https://doi.org/10.3390/molecules25030698

Find Other Styles
Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Article Access Map by Country/Region

1
Search more from Scilit
 
Search
Back to TopTop