57899-96-4 Usage
Uses
Used in Pharmaceutical Development:
AC-LYS-PRO-VAL-NH2 is used as a potential therapeutic agent for its antimicrobial, antiviral, and anticancer effects, making it a candidate for the development of new pharmaceuticals targeting various diseases and conditions.
Used in Biochemical Research:
In the field of biochemical research, AC-LYS-PRO-VAL-NH2 is used as a valuable tool for studying protein-protein interactions, drug-receptor binding, and enzymatic activities due to its unique structure and functional properties.
Used in Antioxidant and Immunomodulatory Applications:
AC-LYS-PRO-VAL-NH2 is used as an antioxidant and immunomodulatory agent, leveraging its potential to combat oxidative stress and modulate immune responses, which can be beneficial in treating a wide range of conditions.
Used in Drug Delivery Systems:
Although not explicitly mentioned in the provided materials, given its potential therapeutic properties, AC-LYS-PRO-VAL-NH2 could also be used in drug delivery systems to improve the efficacy and targeted delivery of pharmaceuticals, similar to the application of gallotannin in overcoming its limitations through novel drug delivery systems.
Check Digit Verification of cas no
The CAS Registry Mumber 57899-96-4 includes 8 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 5 digits, 5,7,8,9 and 9 respectively; the second part has 2 digits, 9 and 6 respectively.
Calculate Digit Verification of CAS Registry Number 57899-96:
(7*5)+(6*7)+(5*8)+(4*9)+(3*9)+(2*9)+(1*6)=204
204 % 10 = 4
So 57899-96-4 is a valid CAS Registry Number.
InChI:InChI=1/C16H32N4O3/c1-5-10-20(16(23)14(18)11(2)3)15(22)13(19-12(4)21)8-6-7-9-17/h11,13-14H,5-10,17-18H2,1-4H3,(H,19,21)/t13-,14-/m0/s1
57899-96-4Relevant academic research and scientific papers
Structural modification of the tripeptide KPV by reductive “glycoalkylation” of the lysine residue
Songok, Abigael C.,Panta, Pradip,Doerrler, William T.,Macnaughtan, Megan A.,Taylor, Carol M.
, (2018/07/03)
Peptides that exhibit enzymatic or hormonal activities are regulatory factors and desirable therapeutic drugs because of their high target specificity and minimal side effects. Unfortunately, these drugs are susceptible to enzymatic degradation, leading to their rapid elimination and thereby demanding frequent dosage. Structurally modified forms of some peptide drugs have shown enhanced pharmacokinetics, improving their oral bioavailability. Here, we discuss a novel glycomimetic approach to modify lysine residues in peptides. In a model system, the ε-amine of Ts-Lys-OMe was reductively alkylated with a glucose derivative to afford a dihydroxylated piperidine in place of the amine. A similar modification was applied to H-KPV-NH2, a tripeptide derived from the α-melanocyte stimulating hormone (α-MSH) reported to have antimicrobial and anti-inflammatory properties. Antimicrobial assays, under a variety of conditions, showed no activity for Ac-KPV-NH2 or the α- or ε-glycoalkylated analogs. Glycoalkylated peptides did, however, show stability toward proteolytic enzymes.
