66638-72-0 Usage
Uses
Used in Biochemistry:
Z-TRP-MET-OH is used as a research tool for studying the roles of tryptophan and methionine in various biochemical processes. Its unique structure allows scientists to investigate the interactions and functions of these amino acids in a controlled manner.
Used in Pharmaceutical Industry:
Z-TRP-MET-OH is used as a potential therapeutic agent for conditions related to the deficiencies or imbalances of tryptophan and methionine. Its combined structure may offer advantages in terms of bioavailability and targeted delivery, potentially leading to more effective treatments.
Used in Nutritional Supplements:
Z-TRP-MET-OH is used as an ingredient in nutritional supplements to support the health benefits associated with tryptophan and methionine. Its combined form may provide a more efficient way to deliver these essential amino acids to the body, promoting overall health and well-being.
Used in Drug Development:
Z-TRP-MET-OH is used as a starting point for the development of new drugs targeting specific health conditions. The unique combination of tryptophan and methionine may offer novel therapeutic opportunities, particularly in the areas of mood regulation, immune function, and cellular metabolism.
Check Digit Verification of cas no
The CAS Registry Mumber 66638-72-0 includes 8 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 5 digits, 6,6,6,3 and 8 respectively; the second part has 2 digits, 7 and 2 respectively.
Calculate Digit Verification of CAS Registry Number 66638-72:
(7*6)+(6*6)+(5*6)+(4*3)+(3*8)+(2*7)+(1*2)=160
160 % 10 = 0
So 66638-72-0 is a valid CAS Registry Number.
66638-72-0Relevant academic research and scientific papers
Suppo, Jean-Simon,Subra, Gilles,Berges, Matthieu,Marcia De Figueiredo, Renata,Campagne, Jean-Marc
, p. 5389 - 5393 (2014)
A mild, practical, and simple procedure for peptide-bond formation is reported. Instead of activation of the carboxylic acid functionality, the reaction involves an unprecedented use of activated α-aminoesters. The method provides a straightforward entry to dipeptides and was effective when a sensitive cysteine residue was used, as no epimerization was detected in this case. The applicability of this method to iterative peptide synthesis was illustrated by the synthesis of a model tetrapeptide in the challenging reverse N→C direction. How to advance by going into reverse: In a mild and practical procedure for peptide-bond formation, free α-aminoesters were activated by treatment with N,N′-carbonyldiimidazole, instead of activating the carboxylic acid functionality (see scheme). The method provided a straightforward route to dipeptides, and its applicability to iterative peptide synthesis was illustrated by the synthesis of a tetrapeptide in the challenging reverse N→C direction.
