85546-27-6 Usage
Uses
Used in Organic Synthesis:
D-Alanine, N-[(1,1-dimethylethoxy)carbonyl]-, 4-nitrophenyl ester is used as a reagent in organic synthesis for the formation of peptide bonds, which are essential for creating proteins and other biologically active molecules.
Used in Peptide Chemistry:
In peptide chemistry, D-Alanine, N-[(1,1-dimethylethoxy)carbonyl]-, 4-nitrophenyl ester is used as a coupling agent to facilitate the formation of peptide bonds between amino acids, contributing to the synthesis of peptides and proteins.
Used in Protecting Group Chemistry:
The 4-nitrophenyl ester group in D-Alanine, N-[(1,1-dimethylethoxy)carbonyl]-, 4-nitrophenyl ester is used as a protecting group in peptide synthesis. It shields specific locations on the peptide chain from unwanted reactions, ensuring the desired peptide sequence is obtained during synthesis.
Used in Biochemistry Research:
D-Alanine, N-[(1,1-dimethylethoxy)carbonyl]-, 4-nitrophenyl ester is a valuable tool in biochemistry research, aiding scientists in understanding the mechanisms of peptide bond formation and the role of protecting groups in peptide synthesis.
Check Digit Verification of cas no
The CAS Registry Mumber 85546-27-6 includes 8 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 5 digits, 8,5,5,4 and 6 respectively; the second part has 2 digits, 2 and 7 respectively.
Calculate Digit Verification of CAS Registry Number 85546-27:
(7*8)+(6*5)+(5*5)+(4*4)+(3*6)+(2*2)+(1*7)=156
156 % 10 = 6
So 85546-27-6 is a valid CAS Registry Number.
85546-27-6Relevant academic research and scientific papers
Rate enhancement and enantioselectivity in ester hydrolysis catalysed by cyclodextrin-peptide hybrids
Tsutsumi, Hiroshi,Hamasaki, Keita,Mihara, Hisakazu,Ueno, Akihiko
, p. 1813 - 1818 (2007/10/03)
A pair of cyclodextrin-peptide hybrids (CD-peptides) having three functional groups, β-cyclodextrin (β-CD), imidazole and carboxylate, in this order and in the reverse order were designed and synthesized as hydrolytic catalysts. These CD-peptides were designed so as to make three functional groups placed on the same side of the α-helix peptide work together. Another pair of CD-peptide hybrids which lack the carboxylate were also designed and synthesized in order to examine the effect of the carboxylate in the novel catalysts. Circular dichroism studies revealed that these CD-peptides have stable α-helix structures and their α-helix contents were high enough (around 70%) to place the functional groups at appropriate positions in the CD-peptides. Boc-D-alanine p-nitrophenyl ester and Boc-L-alanine p-nitrophenyl ester were chosen as substrates and the enantioselectivity of the catalysts in the hydrolysis was examined. Kinetic studies suggested that the presence of carboxylate in the CD-peptides enhances the ester hydrolysis with substrate selectivity.
