4180-62-5 Usage
Uses
Used in Biochemical Research:
Z-GLY-SER-OH is used as a building block for the synthesis of larger peptides and proteins, facilitating the study of their structure, function, and interactions within biological systems.
Used in Pharmaceutical Research and Development:
Z-GLY-SER-OH is used as a component in the development of new drugs, leveraging its specific amino acid sequence to influence biological activity and targeting properties for therapeutic applications.
Used in Drug Delivery Systems:
While not explicitly mentioned in the provided materials, given its role in pharmaceutical research, Z-GLY-SER-OH could potentially be utilized in drug delivery systems to improve the efficacy and bioavailability of drugs by enhancing their delivery to target sites within the body.
Used in Peptide Synthesis:
Z-GLY-SER-OH is used as a starting material or intermediate in the synthesis of specific peptides that may have unique biological functions or serve as therapeutic agents.
Check Digit Verification of cas no
The CAS Registry Mumber 4180-62-5 includes 7 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 4 digits, 4,1,8 and 0 respectively; the second part has 2 digits, 6 and 2 respectively.
Calculate Digit Verification of CAS Registry Number 4180-62:
(6*4)+(5*1)+(4*8)+(3*0)+(2*6)+(1*2)=75
75 % 10 = 5
So 4180-62-5 is a valid CAS Registry Number.
InChI:InChI=1/C13H16N2O6/c16-7-10(12(18)19)15-11(17)6-14-13(20)21-8-9-4-2-1-3-5-9/h1-5,10,16H,6-8H2,(H,14,20)(H,15,17)(H,18,19)
4180-62-5Relevant academic research and scientific papers
Scandium(III) triflate-promoted serine/threonine-selective peptide bond cleavage
Ni, Jizhi,Sohma, Youhei,Kanai, Motomu
supporting information, p. 3311 - 3314 (2017/03/22)
The site-selective cleavage of peptide bonds is an important chemical modification that is useful not only for the structural determination of peptides, but also as an artificial modulator of peptide/protein function and properties. Here we report site-selective hydrolysis of peptide bonds at the Ser and Thr positions with a high conversion yield. This chemical cleavage relies on Sc(iii)-promoted N,O-acyl rearrangement and subsequent hydrolysis. The method is applicable to a broad scope of polypeptides with various functional groups, including a post-translationally modified peptide that is unsuitable for enzymatic hydrolysis. The system was further extended to site-selective cleavage of a native protein, Aβ1-42, which is closely related to the onset of Alzheimer's disease.
