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Human Proteases Annotated Library

Human Proteases Annotated Library Human Proteases Annotated Library Human Proteases Annotated Library Human Proteases Annotated Library Human Proteases Annotated Library
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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
Related

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.
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