169048-84-4

Upstream product

• 100-51-6 benzyl alcohol 
• 83477-74-1 2-R-hydroxysuccinic acid 1-benzylester 

Downstream Products

• 97859-49-9 (R)-5-(hydroxymethyl)-1,3-oxazolidin-2-one 

Relevant academic research and scientific papers

Efficient Pathways to (R)- and (S)-5-Hydroxymethyl-2-oxazolidinone and some Derivatives

2-Oxazolidinones are a very interesting class of compounds due to their various pharmacological effects.Two new syntheses of enantiomerically pure (R)- and (S)-5-hydroxymethyl-2-oxazolidinone have been developed starting with D-mannitol, L-ascorbic acid and (R)- or (S)-malic acid. (R)- and (S)-5-hydroxymethyl-2-oxazolidinone have been used to synthesize some new homochiral 2-oxazolidinone derivatives.

PYRAZOLYL-SUBSTITUTED HETEROARYLS AND THEIR USE AS MEDICAMENTS

The invention relates to new substituted heteroaryls of formula 1 or of formula 1' wherein A is either N or CH, wherein R2 is selected from the group consisting of -C1-3-alkyl, -C1-3-haloalkyl, F, Br, CI, wherein Y is selected from -O- or -CH2-, and wherein R3 is defined as in claim 1, and the pharmaceutically acceptable salts thereof, and the use of these aforementioned compounds for the treatment of diseases such as asthma, COPD, allergic rhinitis, allergic dermatitis, lupus erythematodes, lupus nephritis and rheumatoid arthritis.

NOVEL GLUCOKINASE ACTIVATORS AND METHODS OF USING SAME

Compounds are provided which are phosphonate and phosphinate activators and thus are useful in treating diabetes and related diseases and have the structure wherein is a heteroaryl ring; R4 is —(CH2)n-Z-(CH2)m—PO(OR7)(OR8), —(CH2)nZ-(CH2)m—PO(OR7)Rg, —(CH2)n-Z-(CH2)m—OPO(OR7)Rg, —(CH2)nZ—(CH2)m—OPO(R9)(R10), or —(CH2)nZ—(CH2)m—PO(R9)(R10);R5 and R6 are independently selected from H, alkyl and halogen;Y is R7(CH2)s or is absent; andX, n, Z, m, R4, R5, R6, R7, and s are as defined herein; or a pharmaceutically acceptable salt thereof. A method for treating diabetes and related diseases employing the above compounds is also provided.

Design and synthesis of sulfur based inhibitors of matrix metalloproteinase-1.

Fibroblast collagenase (MMP-1), a member of the matrix metalloproteinases family, is believed to be a pathogenesis of arthritis, by cleaving triple-helical type II collagen in cartilage. From the similarity of the active site zinc binding mode with hydroxamate, we designed and synthesized alpha-mercaptocarbonyl possessing compounds (3-5), which incorporated various peptide sequences as enzyme recognition sites. The P4-P1 peptide incorporating compound (3) exhibited as potent inhibition as the hydroxamate (1) and the carboxylate (2) type inhibitors, with an IC50 of 10(-6) M order against MMP-1. But the inhibitor (3) related compounds (6-8) displayed decreased or no inhibitory potencies. These results suggest that the existence of both the carbonyl and thiol groups might be critical for the inhibition, and the distance between the two functional groups is important for inhibitory potency. For Pn' peptide incorporating compounds (4a-k), except for 4h and 4k, all compounds showed IC50 values under sub-nanomolar. Among them, for potent inhibition, Leu was better than Phe and Val as the P1' amino acid, and the P2' position amino acid was necessary, and preferentially Phe. Insertion of the Pn peptide into 4d or 4k, giving compounds 5a-c, did not increase the activities of 4d and 4k. Substitution of the mercapto group with other functional groups lost the activity of compound 4a. The stereochemical preference at the thiol-attached position was also determined by preparation of both isomers of 4a. It was found that the S configuration compound (36b) is approximately 100 times more potent than the corresponding R-isomer (36a).