Name: Human Proteases Annotated Library
Brand: Arctom Scientific
SKU: CD-SL-000185

Human Proteases Annotated Library

Format & Volume

10 μL/well Solution

30 μL/well Solution

50 μL/well Solution

100 μL/well Solution

Compounds

320

PDF Excel SDF

ATTRIBUTES

Store

Catalog

CD-SL-000185

Brand

ChemDiv

OVERVIEW

Description

•Proteases are enzymatic proteins that cleave specific peptide bonds withing other functional proteins

•Physiologically the protease enzymatic activity can be modulated by

-Mimetics of peptide motifs that bind at a catalytic site
-Chelators of specific metal ions that often used by proteases as cofactors

•Proteases are well recognized as important therapeutic targets for

-Infections, e.g. antibacterial, antiviral, antimalarials
-Inflammatory diseases, e.g. fibrosis, NSAID painkillers, joint stiffness
-Cardiovascular system, e.g. blood pressure regulation, thrombosis

A unique collection of small molecule compounds with annotated activities for Proteases protein targets

Annotated activities : 60 protease targets
Express Delivery : 320 compounds
Complete Version : 2976 compounds

Library Composition

Data sources of annotations : Pharos, ChEMBL 25, PubChem, PubMed, Current Patent Literature (CAS, Integrity)

IDNUMBER – ChemDiv Catalog ID (in some instances the same IDNUMBER might have multiple annotation entries due to multiple data sources or because having activity against multiple similar targets);

UNIPROT – SwissProt and ChEMBL Target accesion ID;

Type – character of the measured activity;

Value – Active compounds selection criteria, included only compounds with reported activities < 5 µM;

pubmed_id – PubMed record entry;

doi, patent_id – journal or patent reference to a publication of original data;

For screening data extracted from PubChem, see column assay_description for entry names PUBCHEM_BIOASSAY

Example of Annotations - an Excel file structure

IDNUMBER	UNIPROT	Target Name	Type	Relation	Value	Units	pubmed_id	doi	patent_id	Target Description	assay_description
8010-3886	P05981	Serine protease hepsin	IC50	=	430	nM			US-9182402-B2	Serine protease hepsin	High-Throughput Screening Assay: To identify novel inhibitors of hepsin (Zhang et al. 1999 J Biomol Screen 4:67)
C050-0376	P07858	Cathepsin B	IC50	=	690	nM	17656088	10.1016/j.bmcl.2007.06.091		Cathepsin B	Inhibition of human liver cathepsin B
R152-2078	P15144	Aminopeptidase N	IC50	=	30	nM	7909847	10.1021/jm00035a014		Aminopeptidase N	Inhibitory potency against aminopeptidase N (APN)
K839-0145	Q9UNA0	ADAMTS5	IC50	=	830	nM	18974001	10.1016/j.bmcl.2008.10.065		A disintegrin and metalloproteinase with thrombospondin motifs 5	Inhibition of ADAMTS5 by FRET assay
P160-0032	P42574	Caspase-3	IC50	=	23	nM	15916416	10.1021/jm048987t		Caspase-3	In vitro inhibitory concentration against human caspase-3
4487-0140	P00749	Urokinase-type plasminogen activator	IC50	=	170	nM	17850059	10.1021/jm070600+		Urokinase-type plasminogen activator	Inhibition of human urokinase
3375-0321	P08253	Matrix metalloproteinase-2	IC50	=	302	nM				72 kDa type IV collagenase	PUBCHEM_BIOASSAY: Dose Response validation of uHTS RPN11 inhibitor hits using a MMP-2 Fluorescence assay. (Class of assay: confirmatory)
3229-1443	P45452	Matrix metalloproteinase 13	IC50	=	640	nM		10.1039/C4MD00556B		Collagenase 3	Inhibition of MMP13 (unknown origin) using Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2 as substrate
V030-2981	P42892	Endothelin-converting enzyme 1	IC50	=	220	nM	16085415	10.1016/j.bmcl.2005.06.085		Endothelin-converting enzyme 1	Inhibitory concentration against endothelin converting enzyme 1 using bradykinin-derived substrate
8015-0649	P43235	Cathepsin K	IC50	=	400	nM	23350811	10.1021/jm3013932		Cathepsin K	Inhibition of human recombinant His-tagged cathepsin K using Cbz-Phe-Arg-AMC as substrate
4234-0237	P00748	Coagulation factor XII	IC50		533	nM				Coagulation factor XII	PUBCHEM_BIOASSAY: Factor XIIa 1536 HTS Dose Response Confirmation. (Class of assay: confirmatory)

Publications

1.J. Med. Chem. 2007 50(20):4928-4938. N-benzoylpyrazoles are novel small-molecule inhibitors of human neutrophil elastase. Schepetkin IA Khlebnikov AI Quinn MT.

2.J. Med. Chem. 2000 43(9):1793-1806. Protease inhibitors: synthesis and QSAR study of novel classes of nonbasic thrombin inhibitors incorporating sulfonylguanidine and O-methylsulfonylisourea moieties at P1. Supuran CT Scozzafava A Briganti F Clare BW.

3.J. Med. Chem. 2009 52(10):3212-3224. Exploration of structure-activity relationship determinants in analogue series. Peltason L Weskamp N Teckentrup A Bajorath J.

4.ACS Med. Chem. Lett. 2013 4(8):699-703. Discovery of Inhibitors of Burkholderia pseudomallei Methionine Aminopeptidase with Antibacterial Activity. Wangtrakuldee P Byrd MS Campos CG Henderson MW Zhang Z Clare M Masoudi A Myler PJ Horn JR Cotter PA Hagen TJ.

5.Bioorg Med Chem 2017 25(3):813-824. Rickettsia prowazekii methionine aminopeptidase as a promising target for the development of antibacterial agents. Helgren TR Chen C Wangtrakuldee P Edwards TE Staker BL Abendroth J Sankaran B Housley NA Myler PJ Audia JP Horn JR Hagen TJ.

6.Bioorg. Med. Chem. Lett. 1999 9(17):2531-2536. Synthesis and structure activity relationships of novel small molecule cathepsin D inhibitors. Dumas J Brittelli D Chen J Dixon B Hatoum-Mokdad H König G Sibley R Witowsky J Wong S.

7.J. Med. Chem. 2014 57(22):9598-9611. Characterization of selective exosite-binding inhibitors of matrix metalloproteinase 13 that prevent articular cartilage degradation in vitro. Spicer TP Jiang J Taylor AB Choi JY Hart PJ Roush WR Fields GB Hodder PS Minond D.

8.MedChemComm 2015 6(5):823-830. Evaluation of the anti-inflammatory/chondroprotective activity of aldose reductase inhibitors in human chondrocyte cultures. Panico A Maccari R Cardile V Avondo S Crasci L Ottana R

9.ACS Med. Chem. Lett. 2013 4(6):565-569. Discovery of a New Class of Potent MMP Inhibitors by Structure-Based Optimization of the Arylsulfonamide Scaffold. Mori M Massaro A Calderone V Fragai M Luchinat C Mordini A.