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Z-β-Ala-NH-cyclohexyl, also known as N-benzyloxycarbonyl-beta-alanine-cyclohexylamide, is a synthetic chemical compound that belongs to the class of peptidomimetics. It is a derivative of beta-alanine, an amino acid, with a cyclohexyl group attached to the nitrogen atom and a benzyloxycarbonyl (Z) protecting group on the amino group. Z-β-Ala-NH-cyclohexyl is often used in organic synthesis and medicinal chemistry, particularly in the design and synthesis of peptide-based drugs and other bioactive molecules. The Z-group serves as a temporary protecting group that can be removed under specific conditions, allowing for further modification or coupling of the molecule. The cyclohexyl moiety provides steric bulk and can influence the conformation and biological activity of the resulting compounds.

16876-65-6

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16876-65-6 Usage

Check Digit Verification of cas no

The CAS Registry Mumber 16876-65-6 includes 8 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 5 digits, 1,6,8,7 and 6 respectively; the second part has 2 digits, 6 and 5 respectively.
Calculate Digit Verification of CAS Registry Number 16876-65:
(7*1)+(6*6)+(5*8)+(4*7)+(3*6)+(2*6)+(1*5)=146
146 % 10 = 6
So 16876-65-6 is a valid CAS Registry Number.

16876-65-6Relevant academic research and scientific papers

Palladium-catalyzed β-C-H arylation of aliphatic aldehydes and ketones using amino amide as a transient directing group

Dong, Cong,Wu, Liangfei,Yao, Jianwei,Wei, Kun

, p. 2085 - 2089 (2019)

This paper describes a new amino-amide-based transient directing group (TDG). The TDG can exhibit better performance in the Pd-catalyzed arylation of aliphatic aldehydes and ketones. This reaction showed good substrate compatibility and regioselectivity. The results indicated that 3-amino-N-isopropylpropionamide was more beneficial to the β-arylation of aliphatic aldehydes than other TDGs under relatively mild conditions.

A Mechanism for bitter Taste Sensibility in Peptides

Ishibashi, Norio,Kouge, Katsushige,Shinoda,Ichizo,Kanehisa, Hidenori,Okai, Hideo

, p. 819 - 828 (2007/10/02)

To estimate the steric distance between the bitter taste determinant sites in peptides, some cyclic dipeptides, amino acid anilides, amino acid cyclohexylamides, and benzoyl amino acids were synthesized and their tastes were evaluated.The diketopiperazine ring of cyclic dipeptides acted as a bitter taste determinant site due to its hydrophobicity.The steric distance between 2 sites was estimated as 4.1 Angstroem from the molecule models of cyclic dipeptides composed of typical amino acids in the bitter peptides.Due to the hypothesis of two bitter taste determinant sites, which bind with the bitter taste receptor via a "binding unit" and a "stimulating unit," a mechanism for the bitterness in peptides was postulated.

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