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Behold Gly-Glu-Gly, a tripeptide showing promising efficacy as a natural anti-inflammatory agent in biomedical contexts. Its potential is grounded in studies that have explored its aptitude for mitigating oxidative stress and inflammation in numerous diseases including rheumatoid arthritis, asthma, and cerebral ischemia/reperfusion injury. The full extent of its therapeutic potential, however, remains a topic of ongoing research and investigation.

Functional Peptides
Catalog number
CAS number
Molecular Formula
Molecular Weight
Size Price Stock Quantity
5 mg $199 In stock
(4S)-4-[(2-aminoacetyl)amino]-5-(carboxymethylamino)-5-oxopentanoic acid
Gly-Glu-Gly; H-GLY-GLU-GLY-OH; glycylglutamylglycine
1.433 g/cm3
Boiling Point
762°C at 760 mmHg
Store at -20°C
InChI Key
Canonical SMILES
1. Bioactive peptides identified from enzymatic hydrolysates of sturgeon skin
Meng Gui, Liang Gao, Lei Rao, Pinglan Li, Ying Zhang, Jia-Wei Han, Jun Li J Sci Food Agric. 2022 Mar 30;102(5):1948-1957. doi: 10.1002/jsfa.11532. Epub 2021 Sep 27.
Background: Recent studies demonstrate that fish byproducts can be used as sources of bioactive peptides for functional foods. Sturgeon skin contains abundant proteins but it has commonly been discarded during sturgeon processing. The objective of the present work was to identify and characterize the bioactive peptides from protein hydrolysates of sturgeon skin. Results: Sturgeon skin protein extract (SKPE) hydrolyzed by flavourzyme for 60 min exhibited high antioxidant activity, dipeptidyl peptidase IV (DPP-IV) and angiotensin converting enzyme (ACE) inhibitory activity. The sequences of peptides from flavourzyme hydrolysates were identified using high-performance liquid chromatography-tandem mass spectrometry. Gly-Asp-Arg-Gly-Glu-Ser-Gly-Pro-Ala (P1) showed the highest DPPH radical scavenging activity (DPPH IC50 = 1.93 mmol L-1 ). Gly-Pro-Ala-Gly-Glu-Arg-Gly-Glu-Gly-Gly-Pro-Arg (P11) (DPP-IV IC50 = 2.14 mmol L-1 ) and Ser-Pro-Gly-Pro-Asp-Gly-Lys-Thr-Gly-Pro-Arg (P12) (DPP-IV IC50 = 2.61 mmol L-1 ) exhibited the strongest DPP-IV inhibitory activity. Gly-Pro-Pro-Gly-Ala-Asp-Gly-Gln-Ala-Gly-Ala-Lys (P6) displayed the highest ACE inhibitory activity (ACE IC50 = 3.77 mmol L-1 ). The molecular docking analysis revealed that DPP-IV inhibition of P11 and P12 are mainly attributed to hydrogen bonds and hydrophobic interactions, whereas ACE inhibition of P6 is mainly attributed to strong hydrogen bonds. Conclusions: These results indicate that SKPE hydrolysates generated by flavourzyme are potential sources of bioactive peptides that could be used in the health food industry. © 2021 Society of Chemical Industry.
2. Influence of aluminum oxide on the prebiotic thermal synthesis of Gly-Glu-(Gly-Glu)(n) polymer
Patricio Leyton, R Antonio Zárate, Sandra Fuentes, Carolina Paipa, Juan S Gómez-Jeria, Yessica Leyton Biosystems. 2011 May-Jun;104(2-3):118-26. doi: 10.1016/j.biosystems.2011.01.008. Epub 2011 Jan 28.
The effect of the aluminum oxide on the thermal synthesis of the glycine-glutamic acid (Gly-Glu-(Gly-Glu)(n) polymer is described. The thermal synthesis in the molten state was carried out in the absence and presence of the oxide. In both cases, the vibrational spectra showed characteristic group frequencies corresponding predominantly to a Gly-Glu-(Gly-Glu)(n) sequence in the polymeric structure. The theoretical spectral data support the experimental proposed Gly-Glu-(Gly-Glu)(n) sequence for the polymer. The SEM-EDX characterization of the solid phase involved in the thermal synthesis showed that the aluminum oxide participates as a site for nucleation and growth of the polymer, explaining the increase of 25% efficiency in the presence of aluminum oxide. Electrophoresis data show shorter polypeptide chains in the presence of aluminum oxide.
3. Formation constants of copper(II) complexes with tripeptides containing Glu, Gly, and His: potentiometric measurements and modeling by generalized multiplicative analysis of variance
Rima Raffoul Khoury, Gordon J Sutton, Diako Ebrahimi, D Brynn Hibbert Inorg Chem. 2014 Feb 3;53(3):1278-87. doi: 10.1021/ic4009575. Epub 2014 Jan 16.
We report a systematic study of the effects of types and positions of amino acid residues of tripeptides on the formation constants logβ, acid dissociation constants pKa, and the copper coordination modes of the copper(II) complexes with 27 tripeptides formed from the amino acids glutamic acid, glycine, and histidine. logβ values were calculated from pH titrations with l mmol L(-1):1 mmol L(-1) solutions of the metal and ligand and previously reported ligand pKa values. Generalized multiplicative analysis of variance (GEMANOVA) was used to model the logβ values of the saturated, most protonated, monoprotonated, logβ(CuL) - logβ(HL), and pKa of the amide group. The resulting model of the saturated copper species has a two-term model describing an interaction between the central and the C-terminal residues plus a smaller, main effect of the N-terminal residue. The model supports the conclusion that two copper coordination modes exist depending on the absence or presence of His at the central position, giving species in which copper is coordinated via two or three fused chelate rings, respectively. The GEMANOVA model for pKamide, which is the same as that for the saturated complex, showed that Gly-Gly-His has the lowest pKamide values among the 27 tripeptides. Visible spectroscopy indicated the formation of metal-ligand dimers for tripeptides His-His-Gly and His-His-Glu, but not for His-His-His, and the formation of multiple ligand bis compexes CuL2 and Cu(HL)2 for tripeptides (Glu/Gly)-His-(Glu/Gly) and His-(Glu/Gly)-(Glu/Gly), respectively.
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