4540-60-7

Upstream product

• 4070-48-8 L-Valine methyl ester 
• 17431-03-7 L-valine ethyl ester 
• 35150-08-4 Boc-Val-NH₂ 
• 13139-28-1 (S)-N-benzyloxycarbonylvalinamide 
• 101301-19-3 Z(OMe)-Val-NH₂ 
• 72-18-4 L-valine 
• 105452-73-1 (S)-2-amino-3-methylbutanenitrile 
• 68858-20-8 Fmoc-Val-OH 
• 115057-38-0 Fmoc-Val-NH₂ 
• 13734-41-3 t-Boc-L-valine 
• 1149-26-4 (S)-N-(benzyloxycarbonyl)valine 
• 3014-80-0 (S)-2-amino-3-methylbutanamide hydrochloride 
• 155486-42-3 (1R,2R,3R,5R)-1-((S)-1-Cyano-2-methyl-propylamino)-5-isopropenyl-2-methyl-cyclohexane-1,3-dicarbonitrile 
• 930779-35-4 9-isopropenyl-2-isopropyl-6-methyl-3-oxo-1,4-diaza-spiro[4.5]decane-7-carbonitrile 

Downstream Products

• 17193-58-7 Z-(β-O-Bz-Asp)-Val-NH2 
• 33900-19-5 Boc-Phe-Val-NH₂ 
• 138093-26-2 <β-(benzylthio)-β,β-dimethylpropionyl>-Tyr(Me)-Phe-Gln-Asn-Cys(Bzl)-Pro-Arg(Tos)-Val-NH2 
• 133201-31-7 <β-(benzylthio)-β,β-pentamethylenepropionyl>-Tyr(Me)-Phe-Gln-Asn-Cys(Bzl)-Pro-Arg(Tos)-Val-NH2 
• 101301-20-6 Z(OMe)-Leu-Val-NH₂ 
• 123197-48-8 H-Phe-Met-Arg-Val-NH₂ 
• 69193-11-9 Z-L-Phe-L-Val-NH₂ 
• 106-48-9 4-chloro-phenol 
• 209047-53-0 N-[4,4',4''-tris(benzoyloxy)trityl]-L-valinamide 
• 712351-43-4 C₂₄H₃₀N₄O₄S₂ 
• 147424-38-2 Z-Val-Gly-Val-NH₂ 
• 147424-37-1 Z-Gly-Val-Val-NH₂ 

Relevant academic research and scientific papers

Preparation method of cannabidiol compound

The invention discloses a preparation method of a compound with a general formula I or pharmaceutically acceptable salts, stereoisomers, esters, prodrugs and solvates thereof, which comprises the following steps: (1) by using a compound A and (1S, 4R) 1methyl 4 (1methyl vinyl) 2cyclohexene 1alcohol as raw materials, carrying out coupling under the action of a chiral imidazolone salt catalyst to obtain a compound B; carrying out sodium sulfite dehalogenation and alkali washing to obtain an intermediate 1; (2) heating the intermediate 1 to 80100 DEG C under the action of DMSO, lithium chloride and an antioxidant, reacting, and recrystallizing to obtain a compound with a general formula I;.

HEMIAMINAL-TAG FOR PROTEIN LABELING AND PURIFICATION

The invention pertains to the synthesis, isolation, and characterization of hemiaminal for selective labeling of peptides, proteins, antibodies, and organic fragments with -C(=0) CH2NH2 and derivatives with -CH2NH2 group over -C(=0) CHRNH2 group (where R≠H). The invention also pertains to the method of single-site immobilization of proteins through N-terminus Gly on solid phase. The invention includes late-stage tagging of N-terminus Gly with an affinity tag, 19F NMR probe, and a fluorophore and a method for metal-free protein purification and isolation of analytically pure proteins.

Synthetic method for chiral alpha-aminoamide compounds

The invention provides a synthetic method for chiral alpha-aminoamide compounds, belongs to the technical field of organic synthetic methodology, and concretely relates to a synthetic method for chiral alpha-aminoamide compounds, wherein the method has a simple process, low costs and good economy. The method comprises the following steps: 1, performing ammonolysis: adding substituted chiral alpha-aminocarboxylate hydrochloride into concentrated ammonia water, performing stirring for 4-12h under a room temperature, wherein each 1mmol substituted chiral alpha-aminocarboxylate hydrochloride is corresponding to 2-8mL the concentrated ammonia water; 2, after a reaction is finished, performing distillation for removing ammonia water after the reaction to obtain crude products chiral alpha-aminoamide compounds; and 3, performing filtration on the obtained crude products chiral alpha-aminoamide compounds by adopting a manner of adding a solvent or performing purification on the obtained crude products chiral alpha-aminoamide compounds through a manner of column chromatography which uses ammonia water as a mobile phase to obtain the products chiral alpha-aminoamide compounds. Compared with the prior art, a large number of an ammonia gas for ammonolysis is not needed in the method, the process and post-treatment are simple, costs are low and reaction time is short.

Derivative of hyaluronic acid modified with amino-carboxylic acid

The present invention provides a hyaluronic acid derivative comprising disaccharide units of Formula (I), and a hyaluronic acid derivative/drug conjugate wherein one or more drugs are conjugated to the hyaluronic acid derivative.

Enantiospecific C-H Activation Using Ruthenium Nanocatalysts

The activation of C-H bonds has revolutionized modern synthetic chemistry. However, no general strategy for enantiospecific C-H activation has been developed to date. We herein report an enantiospecific C-H activation reaction followed by deuterium incorporation at stereogenic centers. Mechanistic studies suggest that the selectivity for the α-position of the directing heteroatom results from a four-membered dimetallacycle as the key intermediate. This work paves the way to novel molecular chemistry on nanoparticles.

"Backdoor Induction" of chirality in asymmetric hydrogenation with rhodium(I) complexes of amino acid substituted triphenylphosphane ligands

This paper describes the synthesis and characterization of 5-(diphenylphosphanyl)isophthalic acid bioconjugates (Lig-[R]2). In addition to symmetrically disubstituted conjugates with amino acids, peptides or amines, a convenient one-pot, two-step procedure for the synthesis of conjugates bearing two different substituents is reported. The 28 prepared phosphanes were used as monodentate ligands in the rhodium(I)-catalyzed hydrogenation of 2-acetamidoacrylate and (Z)-α-acetamidocinnamate. The ligand with the smallest side-chain substituents Lig-[Ala-OMe]2 (1a) revealed the highest selectivity, with up to 84 % ee. The catalysts presented herein are models of artificial metalloenzymes in which the outer-coordination sphere controls the selectivity in catalysis. The chirality of distant hydrogen-bonded amino acids is transmitted by "backdoor induction" to the prochiral RhI center. Models of artificial metalloenzymes are presented in which the outer-coordination sphere controls the selectivity in catalysis. The chirality of distant hydrogen-bonded amino acids or amines is transmitted by "backdoor induction" to the prochiral RhI center. Copyright

Development and evaluation of novel phosphotyrosine mimetic inhibitors targeting the Src homology 2 domain of signaling lymphocytic activation molecule (SLAM) associated protein

Specific interactions between Src homology 2 (SH2) domain-containing proteins and the phosphotyrosine-containing counterparts play significant role in cellular protein tyrosine kinase (PTK) signaling pathways. The SH2 domain inhibitors could potentially serve as drug candidates in treating human diseases. Here we have incorporated a novel phosphotyrosine mimetic, which is an unusual amino acid carrying a cyclosaligenyl (cycloSal) phosphodiester moiety, into dipeptides to investigate the inhibitory effect on SH2 domain-containing proteins. A plate-based assay was also established to screen for inhibitors that disrupt the interaction between a phosphopeptide of SLAM (signaling lymphocytic activation molecule) and its interacting protein SAP (SLAM-associated protein). We identified a number of inhibitors with IC50 values in the range of 17-35 μM, implying that the cycloSal phosphodiester-carrying amino acid could mimic the phosphotyrosyl residue. Our results also raise the possibility of integrating the newly developed phosphotyrosine mimetic moiety into inhibitors designed for other SH2 domain-containing proteins.

Amino acid derived amides and hydroxamic acids as ligands for asymmetric transfer hydrogenation in aqueous media

Amides and hydroxamic acids derived from α-amino acids were evaluated as ligands in combination with rhodium and iridium half-sandwich complexes in asymmetric transfer hydrogenation (ATH) of ketones. The reactions were performed in aqueous media using lithium formate as hydride source. The catalyst systems turned out to be highly efficient and ee's up to 90% were obtained.

Carbamates of 4′-demethyl-4-deoxypodophyllotoxin: Synthesis, cytotoxicity and cell cycle effects

In an attempt to generate compounds with superior bioactivity and reduced toxicity, 12 carbamates of 4′-demethyl-4-deoxypodophyllotoxin, N-(1-oxyl-4′-demethyl- 4-deoxypodophyllic)-α-amino acids amides, were synthesized and evaluated for antiproliferative activity and cell cycle effects. These synthesized compounds proved to be more hydrophilic, as well as improved or comparable in vitro cytotoxicities against four cell lines (A-549, HeLa, SiHa, and HL-60) compared with either parent DPT or anti-cancer drug VP-16. Furthermore, flow cytometric analysis exhibited that N-(1-oxyl-4′- demethyl-4-deoxypodophyllic)-d-α-methine amide (15f) induced cell cycle arrest in the G2/M phase in A-549 cells.

Control of 6-Exo and 7-Endo cyclizations of alkynylamides using platinum and bismuth catalysts

The rules of cyclization: Alkynylamides are regioselectively cycloisomerized into piperazin-2-one and 1,4-diazepan-2-one derivatives by using catalytic amounts of appropriate metal catalysts. A 6-exo-dig addition proceeds in the presence of Bi(OTf)3, while the 7-endo-dig addition occurs with PtCl2 for the same substrate. (see scheme; Ns=o- nitrobenzenesulfonyl, Ts=p-toluenesulfonyl, Cbz=benzyloxycarbonyl, DCE=dichloroethane) Copyright