25840-82-8 Usage
Description
S-Trityl-D-cysteine, a synthetic amino acid derivative, is characterized by its unique structure featuring a trityl group attached to the sulfur atom of D-cysteine. This modification endows it with distinct chemical and biological properties, making it a valuable compound in various applications.
Uses
Used in Pharmaceutical Industry:
S-Trityl-D-cysteine is used as an intermediate in the synthesis of various pharmaceutical compounds. Its unique structure allows for the development of new drugs with potential therapeutic applications.
Used in Medicinal Chemistry:
S-Trityl-D-cysteine is used as a molecular probe to study protein structure and function. Its ability to inhibit the human mitotic kinesin Eg5 makes it a valuable tool in understanding the role of this motor protein in cell division and its potential as a target for anti-cancer therapies.
Used in Drug Development:
S-Trityl-D-cysteine is used as a building block in the design and synthesis of novel bioactive molecules. Its unique properties can be exploited to develop new drugs with improved efficacy and selectivity, particularly in the field of cancer treatment.
Check Digit Verification of cas no
The CAS Registry Mumber 25840-82-8 includes 8 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 5 digits, 2,5,8,4 and 0 respectively; the second part has 2 digits, 8 and 2 respectively.
Calculate Digit Verification of CAS Registry Number 25840-82:
(7*2)+(6*5)+(5*8)+(4*4)+(3*0)+(2*8)+(1*2)=118
118 % 10 = 8
So 25840-82-8 is a valid CAS Registry Number.
25840-82-8Relevant articles and documents
Design, Synthesis, and Conformation-Activity Study of Unnatural Bridged Bicyclic Depsipeptides as Highly Potent Hypoxia Inducible Factor-1 Inhibitors and Antitumor Agents
Koike, Kota,Nagano, Masanobu,Ebihara, Masahiro,Hirayama, Tasuku,Tsuji, Mieko,Suga, Hiroaki,Nagasawa, Hideko
, p. 4022 - 4046 (2020/06/08)
By carrying out structural modifications based on the bicyclic peptide structure of echinomycin, we successfully synthesized various powerful antitumor derivatives. The ring conformation in the obtained compounds was restricted by cross-linking with an unnatural bond. The prepared derivatives were demonstrated to strongly suppress the hypoxia inducible factor (HIF)-1 transcriptional activation and hypoxia induction of HIF-1 protein expression. Particularly, alkene-bridged derivative 12 exhibited remarkably potent cytotoxicity (IC50 = 0.22 nM on the MCF-7 cell line) and HIF-1 inhibition (IC50 = 0.09 nM), which considerably exceeded those of echinomycin. Conformational analyses and molecular modeling studies revealed that the biological activities were enhanced following restriction of the conformation by cross-linking through a metabolically stable and rigid bridge bond. In addition, we proposed a new globular conformation stabilized by intramolecular πstacking that can contribute to the biological effects of bicyclic depsipeptides. The developments presented in the current study serve as a useful guide to expand the chemical space of peptides in drug discovery.
