183665-63-6

Upstream product

• 334-48-5 1-decanoic acid 
• 90719-32-7 (S)-4-Benzyl-2-oxazolidinone 
• 112-13-0 n-decanoyl chloride 
• 101711-90-4 (S)-4-benzyl-2-oxazolidinone lithium salt 

Downstream Products

• 183666-12-8 N-[2(R)-(tert-butylcarboxymethyl)decanoyl]-(S)-4-benzyl-2-oxazolidinone 
• 511550-42-8 (S)-3-((R)-2-Allyl-decanoyl)-4-benzyl-oxazolidin-2-one 
• 510730-53-7 (S)-4-Benzyl-3-((R)-2-benzyloxymethyl-decanoyl)-oxazolidin-2-one 
• 224804-68-6 3-((S)-2-methyldecanoyl)-4(S)-4-benzyloxazolidin-2-one 
• 1204612-25-8 (S)-3-((S)-2-((R)-3-(benzyloxy)-1-hydroxypropyl)decanoyl)-4-benzyloxazolidin-2-one 
• 188359-51-5 (R)-3-((S)-1-Methylcarbamoyl-2-phenyl-ethylcarbamoyl)-undecanoic acid 
• 510730-62-8 (R)-2-Benzyloxymethyl-decanoic acid amide 
• 510730-57-1 (R)-2-Benzyloxymethyl-decanoic acid 

Relevant academic research and scientific papers

Structure-Activity Relationship Study of Majusculamides A and B and Their Analogues on Osteogenic Activity

We discovered that majusculamide A (1) and majusculamide B (2), isolated from a marine cyanobacterium collected in Okinawa, induced osteoblast differentiation in MC3T3-E1 cells. Although majusculamide A (1) has a different configuration only at the C-19 stereocenter, bearing a methyl group, compared to majusculamide B (2), the effect of 1 was stronger than that of 2. We synthesized some analogues of the majusculamides (3-15) and evaluated osteogenic activities of these analogues. The structure-activity relationship study of majusculamide analogues suggested that the number of methyls and configuration at C-19 and the nature of the substituent at C-20 of majusculamide A (1) may be important for the osteoblast differentiation-inducing effect of 1.

Synthesis and use of isotope-labelled substrates for a mechanistic study on human α-methylacyl-CoA racemase 1A (AMACR; P504S)

α-Methylacyl-CoA racemase (AMACR) is an important enzyme for the metabolism of branched-chain lipids and drugs. The enzyme is over-expressed in prostate and other cancers. AMACR 1A, the major splice variant, was purified from recombinant E. coli cells as

Matrix metalloproteinase inhibitors: A structure-activity study

Modifications around the dipeptide-mimetic core of a hydroxamic acid based matrix metalloproteinase inhibitor were studied. These variations incorporated a variety of natural, unnatural, and synthetic amino acids inaddition to modifications of the P1' and P3' substituents. The results of this study indicate the following structural requirements: (2) Potent inhibitorsmust possess string zinc-binding functionalities. (3) The potential importance of the hydrophobic group at position R3 as illustratedby itsability to impart greater relative potency against stromelysin when larger hydrophobic groups are used. (4) Requirements surrounding the nature of the amino acid appear to be more restrictive for stromelysin than for neutrophil collagenase, 72 kDa gelatinase, and 92 kDa gelatinase. These requirements may involve planar fused-ring aryl systems and possibly hydrogen-bonding capabilities.

Inhibition of matrix metalloproteinases: An examination of the S1' pocket

Peptidomimetic carboxylate- and hydroxamate-based inhibitors of matrix metalloproteinases containing extended P1' groups have been prepared. Potent inhibition and good selectivity for MMP-2 has been observed for the compounds produced.