123098-44-2 Usage
Description
Cbz-2-Bromo-D-Phenylalanine is a chemical compound derived from the amino acid phenylalanine, featuring a carbobenzyloxy (Cbz) protective group and a bromine atom at the 2-position of the phenylalanine molecule. It is a versatile building block in organic synthesis and peptide chemistry, used for the preparation of peptide-based drugs and therapeutic agents. Its unique structure and reactivity make it a valuable tool for chemical and pharmaceutical research.
Uses
Used in Pharmaceutical Industry:
Cbz-2-Bromo-D-Phenylalanine is used as a building block for the synthesis of peptide-based drugs and therapeutic agents, contributing to the development of novel compounds with potential biological activity.
Used in Organic Synthesis:
Cbz-2-Bromo-D-Phenylalanine is used as a versatile substrate for the modification of natural amino acids, enabling the creation of new compounds with potential applications in various fields.
Used in Peptide Chemistry:
Cbz-2-Bromo-D-Phenylalanine is utilized in the synthesis of peptides, providing a foundation for the development of peptide libraries for drug discovery and development applications.
Used in Chemical Research:
Due to its unique structure and reactivity, Cbz-2-Bromo-D-Phenylalanine serves as a valuable tool for chemical research, aiding in the exploration of new synthetic pathways and the understanding of molecular interactions.
Check Digit Verification of cas no
The CAS Registry Mumber 123098-44-2 includes 9 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 6 digits, 1,2,3,0,9 and 8 respectively; the second part has 2 digits, 4 and 4 respectively.
Calculate Digit Verification of CAS Registry Number 123098-44:
(8*1)+(7*2)+(6*3)+(5*0)+(4*9)+(3*8)+(2*4)+(1*4)=112
112 % 10 = 2
So 123098-44-2 is a valid CAS Registry Number.
123098-44-2Relevant articles and documents
Superiority of the carbamoylmethyl ester as an acyl donor for the kinetically controlled amide-bond formation mediated by α-chymotrypsin
Miyazawa, Toshifumi,Ensatsu, Eiichi,Yabuuchi, Nobuhiro,Yanagihara, Ryoji,Yamada, Takashi
, p. 390 - 395 (2007/10/03)
The superiority of the carbamoylmethyl ester as an acyl donor for the α-chymotrypsin-catalysed kinetically controlled peptide-bond formation is demonstrated in the couplings of an inherently poor amino acid substrate, Ala, with various amino acid residues as amino components and in the couplings of non-protein amino acids such as halogenophenylalanines as carboxylic components. Furthermore, this approach is applied to the amide-bond formation between an amino acid residue and a chiral amine, which is highly diastereoselective.
Remarkable effects of donor esters on the α-chymotrypsin-catalyzed couplings of inherently poor amino acid substrates
Miyazawa, Toshifumi,Tanaka, Kayoko,Ensatsu, Eiichi,Yanagihara, Ryoji,Yamada, Takashi
, p. 997 - 1000 (2007/10/03)
The extremely low efficiency during the α-chymotrypsin-catalyzed coupling of an inherently poor amino acid substrate, e.g., alanine, using the methyl ester as an acyl donor was significantly improved using esters such as the 2,2,2-trifluoroethyl or carbamoylmethyl ester. The ameliorating effect of the latter ester was especially significant.
