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77457-02-4

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77457-02-4 Usage

Check Digit Verification of cas no

The CAS Registry Mumber 77457-02-4 includes 8 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 5 digits, 7,7,4,5 and 7 respectively; the second part has 2 digits, 0 and 2 respectively.
Calculate Digit Verification of CAS Registry Number 77457-02:
(7*7)+(6*7)+(5*4)+(4*5)+(3*7)+(2*0)+(1*2)=154
154 % 10 = 4
So 77457-02-4 is a valid CAS Registry Number.

77457-02-4Downstream Products

77457-02-4Relevant academic research and scientific papers

(S)-ALPHA-FLUOROMETHYLTYROSINE AS DECARBOXYLASE INHIBITORS FOR USE IN THE TREATMENT OF HYPOTENSION

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Paragraph 0159; 0168, (2021/12/31)

Provided are methods of using and drug delivery systems comprising inhibitors of pathogenic, bacterial metabolite production and conjugates of the inhibitors.

Constraining the Side Chain of C-Terminal Amino Acids in Apelin-13 Greatly Increases Affinity, Modulates Signaling, and Improves the Pharmacokinetic Profile

Tran, Kien,Van Den Hauwe, Robin,Sainsily, Xavier,Couvineau, Pierre,C?té, Jér?me,Simard, Louise,Echevarria, Marco,Murza, Alexandre,Serre, Alexandra,Théroux, Léa,Saibi, Sabrina,Haroune, Lounès,Longpré, Jean-Michel,Lesur, Olivier,Auger-Messier, Mannix,Spino, Claude,Bouvier, Michel,Sarret, Philippe,Ballet, Steven,Marsault, éric

supporting information, p. 5345 - 5364 (2021/02/16)

Side-chain-constrained amino acids are useful tools to modulate the biological properties of peptides. In this study, we applied side-chain constraints to apelin-13 (Ape13) by substituting the Pro12 and Phe13 positions, affecting the binding affinity and signaling profile on the apelin receptor (APJ). The residues 1Nal, Trp, and Aia were found to be beneficial substitutions for Pro12, and the resulting analogues displayed high affinity for APJ (Ki 0.08-0.18 nM vs Ape13 Ki 0.7 nM). Besides, constrained (d-Tic) or α,α-disubstituted residues (Dbzg; d-α-Me-Tyr(OBn)) were favorable for the Phe13 position. Compounds 47 (Pro12-Phe13 replaced by Aia-Phe, Ki 0.08 nM) and 53 (Pro12-Phe13 replaced by 1Nal-Dbzg, Ki 0.08 nM) are the most potent Ape13 analogues activating the Gα12 pathways (53, EC50 Gα12 2.8 nM vs Ape13, EC50 43 nM) known to date, displaying high affinity, resistance to ACE2 cleavage as well as improved pharmacokinetics in vitro (t1/2 5.8-7.3 h in rat plasma) and in vivo.

GENERAL METHOD FOR THE ASYMMETRIC SYNTHESIS OF α-AMINO ACIDS VIA ALKYLATION OF THE CHIRAL NICKEL(II) SCHIFF BASE COMPLEXES OF GLYCINE AND ALANINE

Belokon, Yuri N.,Bakhmutov, Vladimir I.,Chernoglazova, Nina I.,Kochetkov, Konstantin A.,Vitt, Sergei V.,et al.

, p. 305 - 312 (2007/10/02)

Nickel(II) complexes of Schiff bases derived from (S)-o-benzaldehyde and alanine (3), or (S)-O-benzophenone and alanine (4), or glycine (5) have been used for the asymmetric synthesis of α-amino acids under a variety of conditions.The method of choice consists of the reaction of the corresponding complex with the appropriate alkyl halide in DMF at 25 deg C using solid NaOH as a catalyst.Low diastereoselective excess (d.e.) is observed for the alkylation of complex (3) with benzyl bromide and allyl bromide.Large selectivity (80 percent) is observed for the alkylation of complex (4).Optically pure(R)- and (S)-O-benzyl-α-methyl-α-amino acids were obtained (70-90 percent) after the alkylated diastereoisomeric complexes had been seperated on SiO2 and hydrolysed with aqueous HCl.The initial chiral reagents were recovered (80-92 percent).The alkylation of complex (5) gave (S)-alanine, (S)-valine, (S)-phenylalanine, (S)-tryptophan, (S)-isoleucine, (S)-2-aminohexanoic acid, and 3,4-dimethoxyphenylalanine with optical yields of 70-92 percent.The optically pure α-amino acids were obtained after the separation of the alkylated diastereoisomeric complexes on SiO2.The stereochemical mechanism of the alkylation reaction is discussed.

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