KLPGF peptide is a sequence from egg white albumen. This peptide have recently shown interest for Alzheimer’s disease.
Involvement in Alzheimer’s disease
This peptide fragment, KLPGF, demonstrated recently an activity against Acetylcholinesterase (AchE), which is implicated in Alzheimer’s diseases and corresponds to the target of almost all Alzheimer’s disease treatmets. Actually, a deficiency in the brain levels of acetylcholine is seen as key step in the pathogenesis of Alzheimer disease.
Otherwise, KLPGF peptide seems to inhibit the activity of Butyrylcholinesterase (BchE) and Beta-site APP cleaving enzyme 1 (BACE1), which is one of the most promising new therapeutic approaches for Alzheimer’s diseases. Indeed, this receptor induce the formation of Amyloid Beta, a typical peptide from Alzheimer’s diseases.
In a recent study (Zhipeng Yu et al, Biological evaluation and interaction mechanism of beta-site APP cleaving enzyme 1 inhibitory pentapeptide from egg albumin, Food Science and Human Wellness, 2020), molecular docking and Dynamics simulations of peptide KLPGF and BACE1 were performed. It seems that Lys321, Asp228, and Asn233 play important roles in the BACE1 inhibitory peptide design.
KLPGF peptide also shown an antidiabetic activity by inhibiting α-glucosidase and α-amylase.
|Sequence : KLPGF|
|MW : 560,74 g/mol|
|Purity : > 95%|
|Counter-Ion : TFA Salts (see option TFA removal)|
|Delivery format : Freeze dried in propylene 2mL microtubes|
|Peptide Solubility Guideline|
|Bulk peptide quantities available|
|Product catalog||Size||Price € HT||Price $ USD|
1- Yu Z, Yin Y, Zhao W, Liu J, Chen F. Food Chemistry. 2012
Anti-diabetic activity peptides from albumin against α-glucosidase and α-amylaseBACKGROUND : The objectives of this study were to identify novel peptides from albumin, and to evaluate and validate the anti-diabetic activity of peptides against α-glucosidase and α-amylase. In the research, albumin hydrolysate was purified and identified, tandem MS was adapted to characterise the amino acid sequences of peptides from the hydrolysate. In addition, anti-diabetic effects of the peptides with α-glucosidase and α-amylase inhibitory activity have been performed. The present work found eight novel peptides from albumin. Results also suggested that peptide KLPGF had α-glucosidase inhibitory activity with an IC(50) of 59.5±5.7μmoll(-1) and α-amylase inhibitory activity with an IC(50) of 120.0±4.0μmoll(-1). In conclusion, the results revealed that the peptide KLPGF was a potential anti-diabetic inhibitor.
2- Yu Z , Wu S , Zhao W , et al. Food Funct. 2018
Anti-Alzheimers activity and molecular mechanism of albumin-derived peptides against AChE and BChE
Alzheimer’s disease (AD) is a global health issue affecting millions of elderly people worldwide. The aim of the present study was to identify novel anti-AD peptides isolated from albumin. Anti-AD activities of the peptides were evaluated via inhibitory activities on acetylcholinesterase (AChE) and butyrylcholinesterase (BChE). Furthermore, the potential molecular mechanisms of the KLPGF/AChE were investigated by CDOCKER of Discovery studio 2017. The results revealed that peptide KLPGF could effectively inhibit AChE with an inhibition rate of 61.23% at a concentration of 50 μg mL-1. In addition, the peptide KLPGF came in contact with acylation sites and peripheral anion sites of AChE. The present study demonstrates that the peptide KLPGF could become a potential functional food intervention in AD.
3- Zhipeng Yu et al. Food Science and Human Wellness. 2020
Biological evaluation and interaction mechanism of beta-site APP cleaving enzyme 1 inhibitory pentapeptide from egg albumin
Inhibition of beta-site APP cleaving enzyme1 (BACE1) is one of the most promising therapeutic approaches for Alzheimer’s disease. To find natural products for the treatment of Alzheimer’s disease, absorption, distribution, metabolism, excretion and toxicity (ADMET) properties and in vitro BACE1 inhibitory activity of the peptides isolated from egg albumin were evaluated. Then, molecular docking and molecular dynamics simulation were used to explain the molecular mechanism of the interactions between BACE1 and peptides. The IC50 value of peptide KLPGF, with satisfactory ADMET properties, against BACE1 was (8.30 ± 0.56) mmol/L. Molecular docking revealed that KLPGF contacted with the residues of BACE1’s active sites through twelve hydrogen bonds interactions, two hydrophobic interactions, one electrostatic interaction, and two Pi-cation interactions. The 5 ns molecular dynamics simulations confirmed that the structure of KLPGF with BACE1 was stable. Peptide KLPGF contacted the residues Lys321, Asp228, and Asn233 with stable hydrogen bonds. KLPGF may be a potential anti-BACE1 candidate.