75188-89-5 Usage
Uses
Used in Pharmaceutical Research:
H-PRO-LEU-GLY-GLY-OH is used as a research compound for studying the properties and functions of specific amino acid sequences in biological systems. Its role in protein synthesis, structural properties, and neurotransmission can provide insights into the development of new therapeutic agents.
Used in Peptide Synthesis:
In the field of peptide synthesis, H-PRO-LEU-GLY-GLY-OH is used as a building block for creating custom peptides. The protective group (H-) at the beginning of the sequence aids in the controlled synthesis of peptides, ensuring the correct formation of peptide bonds and the desired peptide sequence.
Used in Nutritional Supplements:
H-PRO-LEU-GLY-GLY-OH may be used as a component in nutritional supplements, capitalizing on the benefits of its constituent amino acids. Proline and leucine, in particular, are essential for muscle development and protein synthesis, while glycine contributes to the synthesis of various compounds in the body.
Used in Cosmetics and Skincare:
In the cosmetics and skincare industry, H-PRO-LEU-GLY-GLY-OH could be utilized for its potential benefits in skin health and regeneration. The peptide sequence may play a role in enhancing skin elasticity, hydration, and the overall appearance of the skin.
Used in Agricultural Applications:
H-PRO-LEU-GLY-GLY-OH may also find use in agricultural applications, such as in the development of biopesticides or as a component in fertilizers, leveraging the peptide's potential to stimulate plant growth or improve crop resistance to diseases.
Check Digit Verification of cas no
The CAS Registry Mumber 75188-89-5 includes 8 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 5 digits, 7,5,1,8 and 8 respectively; the second part has 2 digits, 8 and 9 respectively.
Calculate Digit Verification of CAS Registry Number 75188-89:
(7*7)+(6*5)+(5*1)+(4*8)+(3*8)+(2*8)+(1*9)=165
165 % 10 = 5
So 75188-89-5 is a valid CAS Registry Number.
75188-89-5Relevant academic research and scientific papers
Model studies of competing hydrolysis and epimerization of some tetrapeptides of interest in amino acid racemization studies in geochronology
Moir, Michael E.,Crawford, Robert J.
, p. 2903 - 2913 (2007/10/02)
The processes of epimerization of individual peptide units in proteins and the concurrent cleavage of peptide bonds are modelled by heating some tetrapeptide and tetrapeptide derivatives to 148.5 deg C in pH 6.8 phosphate buffer.An excess of D-proline was observed during the heating of L-propyl-L-leucylglycylglycine.The D/L ratio of proline attains a maximum value of 2.1 after 90 minutes.The excess D-proline is attributed to the formation of a 2.3:1 mixture of diketopiperazines cyclo-(D-propyl-L-leucyl) and cyclo-(L-prolyl-L-leucyl).These two species account for most of the leucine and proline in the final mixture after the tetrapeptide is no longer detectable.Only small amounts of prolylleucine can be detcected after 50 hours.It is suggested that the above tetrapeptide undergoes internal aminolysis.Leucine in the tetrapeptide glycyl-L-leucylglycylglycine racemizes three times faster than in L-propyl-L-leucylglycylglycine.This demonstrates that an amino acid residue in a peptide chain does have an effect upon the rate of epimerization of a neighbouring peptide residue.A discussion of the geochemical implications of the results is included.
