70669-15-7

Upstream product

• 13734-41-3 t-Boc-L-valine 
• 2462-32-0 L-phenylalanine benzyl ester hydrochloride 
• 63-91-2 L-phenylalanine 
• 1738-78-9 L-phenylalanine benzyl ester p-toluene-sulfonic acid salt 
• 100-51-6 benzyl alcohol 
• 66617-58-1 N-(tert-butoxycarbonyl)-L-phenylalanine benzyl ester 
• 13734-34-4 N-tert-butoxycarbonyl-L-phenylalanine 
• 962-39-0 L-Phenylalanine benzyl ester 

Downstream Products

• 99429-47-7 Boc-Val-Val-Phe-OBzl 
• 99429-49-9 Val-Val-Phe-OBzl 
• 1026362-29-7 (S)-2-{(S)-2-[(S)-2-(2-Hydroxy-5-nitro-benzoylamino)-3-methyl-butyrylamino]-3-phenyl-propionylamino}-4-methylsulfanyl-butyric acid methyl ester 
• 1026328-79-9 (S)-2-{(S)-2-[(S)-2-(4-Hydroxy-3-methoxy-benzoylamino)-3-methyl-butyrylamino]-3-phenyl-propionylamino}-4-methylsulfanyl-butyric acid methyl ester 
• 1026932-23-9 (S)-2-{(S)-2-[(S)-2-(3-Hydroxy-4-methoxy-benzoylamino)-3-methyl-butyrylamino]-3-phenyl-propionylamino}-4-methylsulfanyl-butyric acid methyl ester 
• 1026037-79-5 (S)-2-{(S)-2-[(S)-2-(2-Hydroxy-4-methoxy-benzoylamino)-3-methyl-butyrylamino]-3-phenyl-propionylamino}-4-methylsulfanyl-butyric acid methyl ester 
• 1027605-22-6 (S)-2-{(S)-2-[(S)-2-(5-Bromo-2-hydroxy-benzoylamino)-3-methyl-butyrylamino]-3-phenyl-propionylamino}-4-methylsulfanyl-butyric acid methyl ester 
• 1026681-56-0 (S)-2-{(S)-2-[(S)-2-(5-Chloro-2-hydroxy-benzoylamino)-3-methyl-butyrylamino]-3-phenyl-propionylamino}-4-methylsulfanyl-butyric acid methyl ester 
• 1027891-65-1 (S)-2-{(S)-2-[(S)-2-(3-Chloro-4-hydroxy-benzoylamino)-3-methyl-butyrylamino]-3-phenyl-propionylamino}-4-methylsulfanyl-butyric acid methyl ester 

Relevant academic research and scientific papers

PROTEASOME INHIBITORS

The disclosure provides proteasome inhibitors that can be used to halt cell division of rapidly dividing cells by preventing the degradation of cell cycle-regulating proteins, such as cyclins, cyclin-dependent kinase inhibitors, and p53. The proteasome in

Design, synthesis, and evaluation of cystargolide-based β-lactones as potent proteasome inhibitors

The peptidic β-lactone proteasome inhibitors (PIs) cystargolides A and B were used to conduct structure-activity relationship (SAR) studies in order to assess their anticancer potential. A total of 24 different analogs were designed, synthesized and evaluated for proteasome inhibition, for cytotoxicity towards several cancer cell lines, and for their ability to enter intact cells. X-ray crystallographic analysis and subunit selectivity was used to determine the specific subunit binding associated with the structural modification of the β-lactone (P1), peptidic core, (Px and Py), and end-cap (Pz) of our scaffold. The cystargolide derivative 5k, structurally unique at both Py and P1, exhibited the most promising inhibitory activity for the β5 subunit of human proteasomes (IC50 = 3.1 nM) and significant cytotoxicity towards MCF-7 (IC50 = 416 nM), MDA-MB-231 (IC50 = 74 nM) and RPMI 8226 (IC50 = 41 nM) cancer cell lines. Cellular infiltration assays revealed that minor structural modifications have significant effects on the ability of our PIs to inhibit intracellular proteasomes, and we identified 5k as a promising candidate for continued therapeutic studies. Our novel drug lead 5k is a more potent proteasome inhibitor than carfilzomib with mid-to-low nanomolar IC50 measurements and it is cytotoxic against multiple cancer cell lines at levels approaching those of carfilzomib.

A multicatalyst system for the one-pot desymmetrization/oxidation of meso-1,2-alkane diols

Two is better than one: We demonstrate the viability of an organocatalytic reaction sequence along a short peptide backbone that carries two independent catalytic functionalities, which allow the rapid, one-pot acylative desymmetrization and oxidation of meso-alkane-1,2-diols to the corresponding acetylated acetoins with good yields and enantioselectivities (see scheme). Copyright

Compounds for enzyme inhibition

Peptide-based compounds including heteroatom-containing, three-membered rings efficiently and selectively inhibit specific activities of N-terminal nucleophile (Ntn) hydrolases associated with the proteasome. The peptide-based compounds include an epoxide

Phenol-derived CVFM analog inhibitors of Ras farnesyltransferase possessing cellular in vitro activity

A study was performed on structure-activity relationships of a series of phenol-derived, CVFM analogs, inhibitors of Ras Farnesyltransferase (FTase). The effect of various substituents on the phenol ring was examined, while the VFM moiety of the potent inhibitor CVFM was kept constant. The FTase inhibitory activity, reported as IC50 in table I, was influenced by both the chemical properties and the relative position of the substituents on the phenolic ring. The most active compounds in this series contained a chloro or bromine substituent on the phenolic ring. Subsequently we have tested the effects of these FTase inhibitors on the anchorage-dependent growth of two rat epithelial cell lines, FRTL-5 and the same line v-Ha-ras transformed. While most of the compounds were inactive, two showed a growth inhibitory effect: compound 4 was active against normal as well against transformed cells while derivative 13 was active only against transformed cells.