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Z-DL-Phe(3F)-OMe is a synthetic chemical compound, specifically a fluorinated derivative of phenylalanine, an essential amino acid. The compound is characterized by the presence of a 3-fluorophenylalanine residue, which is protected by a benzyl (Z) group and a methoxymethyl (OMe) group. This modification introduces a fluorine atom at the 3-position of the phenyl ring, which can significantly alter the chemical and biological properties of the molecule. Z-DL-Phe(3F)-OMe is often used in medicinal chemistry and drug design for the development of new therapeutic agents, as the introduction of fluorine can enhance the stability, lipophilicity, and metabolic profile of the compound. The DL-configuration indicates that the compound is a racemic mixture, containing both the D and L isomers of the amino acid.

49759-56-0

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49759-56-0 Usage

Check Digit Verification of cas no

The CAS Registry Mumber 49759-56-0 includes 8 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 5 digits, 4,9,7,5 and 9 respectively; the second part has 2 digits, 5 and 6 respectively.
Calculate Digit Verification of CAS Registry Number 49759-56:
(7*4)+(6*9)+(5*7)+(4*5)+(3*9)+(2*5)+(1*6)=180
180 % 10 = 0
So 49759-56-0 is a valid CAS Registry Number.

49759-56-0Relevant academic research and scientific papers

α-chymotrypsin-catalysed peptide synthesis via the kinetically controlled approach using activated esters as acyl donors in organic solvents with low water content: Incorporation of non-protein amino acids into peptides

Miyazawa, Toshifumi,Nakajo, Shin'ichi,Nishikawa, Miyako,Hamahara, Kazumi,Imagawa, Kiwamu,Ensatsu, Eiichi,Yanagihara, Ryoji,Yamada, Takashi

, p. 82 - 86 (2007/10/03)

The α-chymotrypsin-catalyzed peptide synthesis via the kinetically controlled approach using activated esters as acyl donors in orgnanic solvents with low water content was presented. The methyl esters of N-Z derivatives of racemic non-protein amino acids were chosen as carboxy components. They allowed the peptide-bond formation and optical resolution simultaneously to yield homochiral peptides. This method is useful for the incorporation of non-protein amino acids into peptides.

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