112245-04-2

Basic information

• Product Name: Butanedioic acid, 2-(2-Methylpropyl)-, 4-(1,1-diMethylethyl) ester, (2R)-
• Synonyms: Butanedioic acid, 2-(2-Methylpropyl)-, 4-(1,1-diMethylethyl) ester, (2R)-;(2R)-4-methyl-2-[2-[(2-methylpropan-2-yl)oxy]-2-oxoethyl]pentanoic acid;(2R)-2-[(tert-Butoxycarbonyl)methyl]-4-(methyl)pentanoic acid;(R)-2-(2-(tert-Butoxy)-2-oxoethyl)-4-methylpentanoic acid
• CAS NO: 112245-04-2
• Molecular Formula: C₁₂H₂₂O₄
• Molecular Weight: 230.30068
• Mol File: 112245-04-2.mol

Chemical Properties

• Boiling Point: 324.7±25.0 °C(Predicted)
• Appearance: /
• Density: 1.021±0.06 g/cm3(Predicted)
• Storage Temp.: 2-8°C
• PKA: 4.50±0.23(Predicted)
• CAS DataBase Reference: Butanedioic acid, 2-(2-Methylpropyl)-, 4-(1,1-diMethylethyl) ester, (2R)-(CAS DataBase Reference)
• NIST Chemistry Reference: Butanedioic acid, 2-(2-Methylpropyl)-, 4-(1,1-diMethylethyl) ester, (2R)-(112245-04-2)
• EPA Substance Registry System: Butanedioic acid, 2-(2-Methylpropyl)-, 4-(1,1-diMethylethyl) ester, (2R)-(112245-04-2)

Safety Data

• Hazardous Substances Data: 112245-04-2(Hazardous Substances Data)

Upstream product

• 38136-29-7 4-methylvaleroyl chloride 
• 646-07-1 4-Methylpentanoic acid 
• 112106-12-4 4-tert.butyl 1-(4nitrobenzyl) 2(R)-isobutylsuccinate 
• 184948-24-1 tert-butyl (2R)-1,2-dibenzyl 4-methylpentane-1,1,2-tricarboxylate 
• 130317-28-1 benzyl 2R-trifluoromethanesulfonyloxy-4-methylvalerate 
• 37755-48-9 benzyl (R)-2-hydroxy-4-methylpentanoate 
• 20312-37-2 (R)-2-hydroxy-4-methylpentanoic acid 
• 113543-30-9 (S)-4-benzyl-3-(4-methylpentanoyl)oxazolidin-2-one 
• 5292-43-3 bromoacetic acid tert-butyl ester 
• 144287-83-2 (R)-tert-butyl 3-((S)-4-benzyl-2-oxooxazolidine-3-carbonyl)-5-methylhexanoate 
• 219616-31-6 2-(tert-butoxycarbonyl)-(3R)-3-isobutylsuccinic acid 

Downstream Products

• 1351523-43-7 (R)-3-(cyclopropyl(4-(2-(6-methoxypyridin-3-yl)phenyl)thiazol-2-yl)carbamoyl)-5-methyl hexanoic acid 
• 1351523-58-4 (R)-3-((4-(2-(6-(1H-pyrazol-1-yl)pyridin-3-yl)phenyl)thiazol-2-yl)(cyclopropyl)carbamoyl)-5-methylhexanoic acid 
• 183665-96-5 [(S)-3-((2R,3S)-3-Benzyloxycarbamoyl-2-isobutyl-hex-5-enoylamino)-2-oxo-azepan-1-yl]-acetic acid methyl ester 
• 183665-92-1 {(S)-3-[(R)-2-((S)-1-Benzyloxycarbamoyl-ethyl)-4-methyl-pentanoylamino]-2-oxo-azepan-1-yl}-acetic acid methyl ester 
• 210484-26-7 2-{(R)-1-[(S)-2-(4-Hydroxy-phenyl)-1-methylcarbamoyl-ethylcarbamoyl]-3-methyl-butyl}-hex-5-enoic acid tert-butyl ester 
• 211630-68-1 (2S,3R)-2-Allyl-2,5-dimethyl-3-((S)-1-methylcarbamoyl-2-phenyl-ethylcarbamoyl)-hexanoic acid tert-butyl ester 

Relevant articles and documents

Selective non-zinc binding MMP-2 inhibitors: Novel benzamide Ilomastat analogs with anti-tumor metastasis

Novel Ilomastat analogs with substituted benzamide groups, instead of hydroxamic acid groups, were designed, synthesized and evaluated against MMP-2 and MMP-9. Among these analogs, the most potent compound 10a exhibited potent inhibitory activity against

Hydroxamate-Based Selective Macrophage Elastase (MMP-12) Inhibitors and Radiotracers for Molecular Imaging

Macrophage elastase [matrix metalloproteinase (MMP)-12] is the most upregulated MMP in abdominal aortic aneurysm (AAA) and, hence, MMP-12-targeted imaging may predict AAA progression and rupture risk. Here, we report the design, synthesis, and evaluation of three novel hydroxamate-based selective MMP-12 inhibitors (CGA, CGA-1, and AGA) and the methodology to obtain MMP-12 selectivity from hydroxamate-based panMMP inhibitors. Also, we report two 99mTc-radiotracers, 99mTc-AGA-1 and 99mTc-AGA-2, derived from AGA. 99mTc-AGA-2 displayed faster blood clearance in mice and better radiochemical stability compared to 99mTc-AGA-1. Based on this, 99mTc-AGA-2 was chosen as the lead tracer and tested in murine AAA. 99mTc-AGA-2 uptake detected by autoradiography was significantly higher in AAA compared to normal aortic regions. Specific binding of the tracer to MMP-12 was demonstrated through ex vivo competition. Accordingly, this study introduces a novel family of selective MMP-12 inhibitors and tracers, paving the way for further development of these agents as therapeutic and imaging agents.

N-Thiazolylamide-based free fatty-acid 2 receptor agonists: Discovery, lead optimization and demonstration of off-target effect in a diabetes model

Free fatty acid-2 (FFA2) receptor is a G-protein coupled receptor of interest in the development of therapeutics in metabolic and inflammatory disease areas. The discovery and optimization of an N-thiazolylamide carboxylic acid FFA2 agonist scaffold is described. Dual key objectives were to i) evaluate the potential of this scaffold for lead optimization in particular with respect to safety de-risking physicochemical properties, i.e. lipophilicity and aromatic content, and ii) to demonstrate the utility of selected lead analogues from this scaffold in a pertinent in vivo model such as oral glucose tolerance test (OGTT). As such, a concomitant improvement in bioactivity together with lipophilic ligand efficiency (LLE) and fraction sp3 content (Fsp3) parameters guided these efforts. Compound 10 was advanced into studies in mice on the basis of its optimized profile vs initial lead 1 (ΔLLE = 0.3, ΔFsp3 = 0.24). Although active in OGTT, 10 also displayed similar activity in the FFA2-knockout mice. Given this off-target OGTT effect, we discontinued development of this FFA2 agonist scaffold.

Coupling protein engineering with probe design to inhibit and image matrix metalloproteinases with controlled specificity

Matrix metalloproteinases (MMPs) are zinc endopeptidases that play roles in numerous pathophysiological processes and therefore are promising drug targets. However, the large size of this family and a lack of highly selective compounds that can be used for imaging or inhibition of specific MMPs members has limited efforts to better define their biological function. Here we describe a protein engineering strategy coupled with small-molecule probe design to selectively target individual members of the MMP family. Specifically, we introduce a cysteine residue near the active-site of a selected protease that does not alter its overall activity or function but allows direct covalent modification by a small-molecule probe containing a reactive electrophile. This specific engineered interaction between the probe and the target protease provides a means to both image and inhibit the modified protease with absolute specificity. Here we demonstrate the feasibility of the approach for two distinct MMP proteases, MMP-12 and MT1-MMP (or MMP-14).

NOVEL COMPOUNDS, PHARMACEUTICAL COMPOSITION AND METHODS FOR USE IN TREATING METABOLIC DISORDERS

The present invention is directed to novel compounds of formula (I) and their use in treating metabolic diseases.

Tetrazolylpropionamides as inhibitors of Abeta protein production

This invention relates to novel tetrazolylpropionamides in which the amide group comprises an aminoazepinone, and related structures, of Formula (I): or pharmaceutically acceptable salt or prodrug forms thereof, their pharmaceutical compositions and metho

Improved gelatinase a selectivity by novel zinc binding groups containing galardin derivatives

The synthesis of several analogues of galardin, a MMP inhibitor, are presented with their in vitro inhibitory activity against MMP-1 and MMP-2. These compounds contain a distinct Zinc Binding Group (ZBG). Those having a 2-acylated-heterocycle as well as a 2-arylamide function do not exhibit a good inhibition/selectivity against the enzymes tested. On the contrary, those that are based on a hydrazide scaffold present potent selectivity for MMP-2 versus MMP-1.

Matrix metalloprotease inhibitors

Compounds of formula (I) and their pharmaceutically acceptable salts inhibit matrix metalloproteases, such as stromelysin, gelatinase, matrilysin and collagenase, and are useful in the treatment of mammals having disease-states alleviated by the inhibition of such matrix metalloproteases.

Matrix metalloprotease inhibitors

Compounds of formula (I): STR1 as single stereoisomers or mixtures thereof and their pharmaceutically acceptable salts inhibit matrix metalloproteases, such as interstitial collagenases, and are useful in the treatment of mammals having disease states alleviated by the inhibition of such matrix metalloproteases, for example arthritic diseases or bone resorption disease, such as osteoporosis.

CYSTEINE PROTEASE INHIBITORS

The present invention relates to cysteine protease inhibitors of the general formula (I): STR1 wherein Z is a cysteine protease binding moiety; X and Y are S, O or optionally substituted N; and R 1 is optionally substituted alkyl or aryl.