52558-23-3

Upstream product

• 24424-99-5 di-tert-butyl dicarbonate 
• 1154758-41-4 (R)-ethyl 3-azido-2-hydroxypropionate 
• 111651-48-0 (R)-3-azido-2-hydroxypropionic acid 
• 632-11-1 (R)-3-amino-2-hydroxypropanoic acid 
• 219325-41-4 (5-oxo-[1,3]dioxolan-4-ylmethyl)-carbamic acid tert-butyl ester 

Downstream Products

• 458531-94-7 N^α-[3-(tert-butyloxycarbonyl)-2(R)-hydroxypropionyl]-leucyl-O-methyl-tyrosine N-methylamide 
• 1154758-42-5 6'-trifluoroacetyl-2',3-diPNZ-1-((R)-3-(tert-butoxycarbonylamino)-2-hydroxy-propionyl)-sisomicin 
• 458531-96-9 N^α-[3-(tert-butyloxycarbonyl)-2(S)-(acetylsulfanyl)propionyl]-leucyl-O-methyl-tyrosine N-methylamide 
• 219325-39-0 benzoic acid 2-tert-butoxycarbonylamino-1-carboxy-ethyl ester 

Relevant academic research and scientific papers

?-LACTAMASE INHIBITOR AND USE THEREOF

Provided are a β-lactamase inhibitor of formula (I), or an ester, a stereoisomer or a pharmaceutically acceptable salt thereof, and a method of preparing the same. Further provided is a pharmaceutical composition comprising the β-lactamase inhibitor of formula (I), or the ester, the stereoisomer or pharmaceutically acceptable salt thereof. In addition, the present invention relates to a method for treating diseases caused by bacterial infection, which comprises administering the β-lactamase inhibitor of formula (I), or the ester, the stereoisomer or the pharmaceutically acceptable salt thereof to a patient or a subject in need.

NOVEL BRADYKININ B2 RECEPTOR ANTAGONISTS

The invention relates to a compound according to general formula (I), which acts as a bradykinin (BK) B2 receptor antagonist; to a pharmaceutical composition containing one or more of the compound(s) of the invention; to a combination preparation containing at least one compound of the invention and at least one further active pharmaceutical ingredient; and to uses of said compound(s), including the use as a medicament.

TREATMENT OF URINARY TRACT INFECTIONS WITH ANTIBACTERIAL AMINOGLYCOSIDE COMPOUNDS

A method for treating a urinary tract infection in a mammal in need thereof is disclosed, the method comprising administering to the mammal an effective amount of an antibacterial aminoglycoside compound.

ANTIBACTERIAL AMINOGLYCOSIDE ANALOGS

Compounds of structure (I): having antibacterial activity are disclosed, including stereoisomers, pharmaceutically acceptable salts and prodrugs thereof, wherein Q1, Q2, Q3, R8 and R9 are as defined herein. Methods associated with preparation and use of such compounds, as well as pharmaceutical compositions comprising such compounds, are also disclosed.

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).

Studies related to the absolute configuration of cyclocinamide A: Total synthesis of 4(R),11(R)-cyclocinamide A

Coupling of the fluorenylmethyl ester 3 (R = Fm) of (S)-5- bromotryptophan with N(α)-BOC-(S)-asn-O-benzoyl-(R)-ise 9 gave rise to tripeptide 10. Cleavage of the BOC group in 10 followed by coupling with N(α)-BOC-N(β)-Fmoc-(R)-2,3-diaminopropanoic acid afforded tetrapeptide 11 which was transformed into cyclic peptide 12. Cleavage of the BOC in 12 followed by coupling with the glycine derived side chain 14 gave rise, after removal of the benzoyl group to 4(R),11(R)-cyclocinamide A(2) which was not identical to natural cyclocinamide A(1), suggesting that 1 possesses the 4(S),7(S),11(S),14(S) configuration.