ilomastat

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| Name = GM6001

| ImageFile = Ilomastat.svg

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| PIN = (3R)-N1-Hydroxy-N4-{(1S)-1-[(1H-indol-3-yl)methyl]-2-(methylamino)-2-oxoethyl}-3-(2-methylpropyl)butanediamide

| OtherNames = Galardin, GM6001

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| Abbreviations = GM6

| CASNo = 142880-36-2

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| UNII = I0403ML141

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| PubChem = 132519

| ChemSpiderID = 117009

| SMILES = CC(C)C[C@H](CC(=O)NO)C(=O)N[C@@H](CC1=CNC2=CC=CC=C21)C(=O)NC

| InChI = 1S/C20H28N4O4/c1-12(2)8-13(10-18(25)24-28)19(26)23-17(20(27)21-3)9-14-11-22-16-7-5-4-6-15(14)16/h4-7,11-13,17,22,28H,8-10H2,1-3H3,(H,21,27)(H,23,26)(H,24,25)/t13-,17+/m1/s1

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| MeSHName = GM6001

| DrugBank = DB02255

| ChEBI = 137236

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| C=20 | H=28 | N=4 | O=4

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Ilomastat (INN),{{cite web|title=International Nonproprietary Names for Pharmaceutical Substances (INN). Recommended International Nonproprietary Names: List 36|url=https://www.who.int/medicines/publications/druginformation/innlists/RL36.pdf|publisher=World Health Organization|access-date=23 February 2017|page=148}} (codenamed GM6001, proprietary name Galardin®) is a broad-spectrum matrix metalloproteinase inhibitor.{{cite journal |vauthors=Grobelny D, Poncz L, Galardy RE | title = Inhibition of human skin fibroblast collagenase, thermolysin, and Pseudomonas aeruginosa elastase by peptide hydroxamic acids | journal = Biochemistry | volume = 31 | issue = 31 | pages = 7152–4 |date=August 1992 | pmid = 1322694 | doi = 10.1021/bi00146a017}}{{cite journal |vauthors=Schultz GS, Strelow S, Stern GA, Chegini N, Grant MB, Galardy RE, Grobelny D, Rowsey JJ, Stonecipher K, Parmley V | title = Treatment of alkali-injured rabbit corneas with a synthetic inhibitor of matrix metalloproteinases | journal = Invest. Ophthalmol. Vis. Sci. | volume = 33 | issue = 12 | pages = 3325–31 |date=November 1992 | pmid = 1385350 }}{{cite journal |vauthors=Santiskulvong C, Rozengurt E | title = Galardin (GM 6001), a broad-spectrum matrix metalloproteinase inhibitor, blocks bombesin- and LPA-induced EGF receptor transactivation and DNA synthesis in rat-1 cells | journal = Exp. Cell Res. | volume = 290 | issue = 2 | pages = 437–46 |date=November 2003 | pmid = 14568001 | doi = 10.1016/S0014-4827(03)00355-0}}

This chemotherapy agent is considered to have application in skincare products for its antiaging properties.

Ilomastat is a member of the hydroxamic acid class of reversible metallopeptidase inhibitors. The anionic state of the hydroxamic acid group forms a bidentate complex with the active site zinc.{{cite web | url = http://merops.sanger.ac.uk/cgi-bin/smi_summary?mid=J16.402 | archive-url = https://archive.today/20121223040118/http://merops.sanger.ac.uk/cgi-bin/smi_summary?mid=J16.402 | url-status = dead | archive-date = December 23, 2012 | title = Small-molecule inhibitor J16.402: galardin | publisher = Wellcome Trust Sanger Institute | work = MEROPS - the Peptidase Database | date = 2010-09-07 | access-date = 2010-10-04 }}

Examples of enzymes that ilomastat inhibit include rabbit MMP9,{{cite journal | pmid = 1655675 | volume=32 | title=An inhibitor of the matrix metalloproteinase synthesized by rabbit corneal epithelium | year=1991 | journal=Invest Ophthalmol Vis Sci | pages=2997–3001 | vauthors=Fini ME, Cui TY, Mouldovan A, Grobelny D, Galardy RE, Fisher SJ| issue=11 }} thermolysin, peptide deformylase,{{cite journal |vauthors=Balakrishnan A, Patel B, Sieber SA, Chen D, Pachikara N, Zhong G, Cravatt BF, Fan H | title = Metalloprotease inhibitors GM6001 and TAPI-0 inhibit the obligate intracellular human pathogen Chlamydia trachomatis by targeting peptide deformylase of the bacterium | journal = J. Biol. Chem. | volume = 281 | issue = 24 | pages = 16691–9 |date=June 2006 | pmid = 16565079 | doi = 10.1074/jbc.M513648200 | doi-access = free }} and anthrax lethal factor endopeptidase (LF) produced by the bacterium Bacillus anthracis.{{cite journal |vauthors=Kocer SS, Walker SG, Zerler B, Golub LM, Simon SR | title = Metalloproteinase inhibitors, nonantimicrobial chemically modified tetracyclines, and ilomastat block Bacillus anthracis lethal factor activity in viable cells | journal = Infect. Immun. | volume = 73 | issue = 11 | pages = 7548–57 |date=November 2005 | pmid = 16239558 | pmc = 1273843 | doi = 10.1128/IAI.73.11.7548-7557.2005 }}{{PDB|1PWU}}; {{cite journal |vauthors=Turk BE, Wong TY, Schwarzenbacher R, Jarrell ET, Leppla SH, Collier RJ, Liddington RC, Cantley LC | title = The structural basis for substrate and inhibitor selectivity of the anthrax lethal factor | journal = Nat. Struct. Mol. Biol. | volume = 11 | issue = 1 | pages = 60–6 |date=January 2004 | pmid = 14718924 | doi = 10.1038/nsmb708 | s2cid = 39119275 }}

References