46741-65-5

Upstream product

• 328-38-1 (R)-leucine 
• 100-51-6 benzyl alcohol 
• 16937-99-8 N-Boc-D-Leu 
• 100-39-0 benzyl bromide 
• 80089-22-1 L-leucine (phenylmethyl)ester 
• 17664-93-6 (R)-benzyl 2-amino-4-methylpentanoate p-toluenesulfonate salt 
• 158804-50-3 Boc-D-leucine benzyl ester 

Downstream Products

• 849833-82-5 N-(2-Boc-aminoethyl)-D-leucine benzyl ester 
• 926648-85-3 (5R)-4-(benzyloxy)-5-isobutyl-1,5-dihydro-2H-pyrrol-2-one 
• 849833-84-7 N-(2-Boc-aminoethyl)-N-(thymin-1-ylacetyl)-D-leucine benzyl ester 
• 38689-30-4 L-leucyl-L-leucine 
• 1296838-31-7 (D-L)2-OBn 
• 952-43-2 (3R,6R)-3,6-diisobutylpiperazine-2,5-dione 
• 328-38-1 (R)-leucine 
• 195708-10-2 (R)-2-[(azepane-1-carbonyl)-amino]-4-methyl-pentanoic acid benzyl ester 
• 204274-96-4 N-benzyloxy-2(R)-<<(S)-methylphenylphosphinyl>benzylamino>-4-methylpentanamide 

Relevant academic research and scientific papers

COMPOSITIONS AND METHODS FOR CYCLOFRUCTANS AS SEPARATION AGENTS

The present invention relates to derivatized cyclofructan compounds, compositions comprising derivatized cyclofructan compounds, and methods of using compositions comprising derivatized cyclofructan compounds for chromatographic separations of chemical species, including enantiomers. Said compositions may comprise a solid support and/or polymers comprising derivatized cyclofructan compounds.

Phosphorus ylide based functionalizations of tetronic and tetramic acids

The versatility of the ylide (triphenylphosphoranylidene)ketene (Ph 3P=C=C=O, 3) in the construction of tetronic and tetramic acids from various carboxylic acid derivatives is demonstrated by new reactions and extensions of known ones. With α-h

Methods and compositions for treating amyloid-related diseases

Methods, compounds, pharmaceutical compositions and kits are described for treating or preventing amyloid-related disease.

Effect of PNA backbone modifications on cyanine dye binding to PNA-DNA duplexes investigated by optical spectroscopy and molecular dynamics simulations

Optical spectroscopy and molecular dynamics simulations have been used to study the interaction between a cationic cyanine dye and peptide nucleic acid (PNA)-DNA duplexes. This recognition event is important because it leads to a visible color change, signaling successful hybridization of PNA with a complementary DNA strand. We previously proposed that the dye recognized the minor groove of the duplex, using it as a template for the assembly of a helical aggregate. Consistent with this, we now report that addition of isobutyl groups to the PNA backbone hinders aggregation of the dye when the substituents project into the minor groove but have a weaker effect if directed out of the groove. UV-Visible and circular dichroic spectroscopy were used to compare aggregation on the different PNA-DNA duplexes, while molecular dynamics simulations were used to confirm that the substituents block the minor groove to varying degrees, depending on the configuration of the starting amino acid. In addition to a simple steric blockage effect of the substituent, the simulations suggest that directing the isobutyl group into the minor groove causes the groove to narrow and the duplex to become more rigid, structural perturbations that are relevant to the growing interest in backbone-modified PNA for applications in the biological and materials sciences.

PHOSPHINIC ACID AMIDES AS MATRIX METALLOPROTEASE INHIBITORS

The invention provides compounds which are useful as inhibitors of matrix metalloproteases, and which are effective in treating conditions characterized by excess activity of these enzymes. In particular, the present invention relates to a compound having

Peptide nucleic acids (PNAs) with a functional backbone

The synthesis of 10 new T-PNA monomers derived from L-amino acids is presented. The monomers were incorporated into decameric PNA oligomers, and the hybridisation with RNA, DNA and PNA complements studied by thermal stability measurements.

PHOSPHINIC ACID AMIDES AS MATRIX METALLOPROTEASE INHIBITORS

The invention provides compounds which are useful as inhibitors of matrix metalloproteases, and which are effective in treating conditions characterized by excess activity of these enzymes. In particular, the present invention relates to a compound having

ANTIHERPETIC AGENTS

A series of carboxyl-containing N-alkyldipeptides have been found to posess antiviral potency-specifically against herpes simplex virus-by selectively inhibiting the viral ribonucleotide reductase enzyme

Enzymes in organic synthesis: Use of subtilisin and a highly stable mutant derived from multiple site-specific mutations

A subtilisin mutant (subtilisin 8350) derived from subtilisin BPN' via six-specific mutations (Met50Phe, Gly169Ala, Asn76Asp, Gln206Cys, Tyr217Lys, and Asn218Ser) was found to be 100 times more stable than the wild-type enzyme in aqueous solution at room temperature and 50 times more stable than the wild type in anhydrous dimethylformamide. Kinetic studies using ester, thio ester, and amide substrates, and the transition-state analogue inhibitor Boc-Ala-Val-Phe-CF3, indicate the both the wild-type and the mutant enzymes have very similar specificities and catalytic properties. The inhibition constant (K(i)) = 5.0 μM) for the wild-type enzyme is approximately 5 times that of the mutant enzyme (K(i)) = 1.1 μM), suggesting that the mutant enzyme binds the reaction transition state more strongly than the wild-type enzyme. This result is consistent with the observed rate constants for the corresponding ester and amide substrates; i.e. the k(cat)/k(m) values for the mutant are larger than those for hhe wild-type enzyme. Application of the mutant enzyme and the wild-type enzyme to organic synthesis has been demonstrated in the regioselective acylation of nucleosides in anhydrous dimethylformamide (with 65-100% regioselectivity at the 5'-position), in the enantioselective hydrolysis of N-protected and unprotected common and uncommon amino acid esters in water (with 85-98% enantioselectivity for the L-isomer), and in the synthesis of di- and oligopeptides via aminolysis of N-protected amino acid and peptide esters. The enzymatic peptide synthesis was carried out under high concentrations of DMF (~50%) to improve substrate solubility and to minimize enzymatic peptide cleavage. Low enantioselectivity was observed in the enzymatic transformation of non-amino acid alcohols and acids.