Ovotransferrin 328-332, also called Conalbumin 328-332, is a part of the egg white albumen.
RVPSL peptide has been described to have a protective activity on the blood pressure by inhibiting the Angiotensin-Converting Enzyme (ACE). Ovotransferrin 328-332 peptide would be a serious drug candidate, as powerful as current drugs and without side effects.
Involvement in Alzheimer’s disease
This peptide fragment demonstrated recently an activity against Acetylcholinesterase (AchE), which is implicated in Alzheimer’s diseases. Actually, a deficiency in the brain levels of acetylcholine is seen as key step in the pathogenesis of Alzheimer disease.
Otherwise, Ovostransferrin 328-332 seems to be involved in a possible inhibition of beta-site APP clieaving 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.
|Sequence : RVPSL|
|MW : 570.69 g/mol (C25H46N8O7)|
|Purity : > 95%|
|Counter-Ion : TFA Salts (see option TFA removal)|
|Delivery format : Freeze dried in propylene 2mL microtubes|
|Other Names : Conalbumin (328-332), 1226776-54-0, RVPSL peptide|
|Peptide Solubility Guideline|
|Bulk peptide quantities available|
|Product catalog||Size||Price € HT||Price $ USD|
1- Ding L, Wang L, Zhang Y, Liu J. J Agric Food Chem. (2015)
Transport of Antihypertensive Peptide RVPSL, Ovotransferrin 328-332, in Human Intestinal Caco-2 Cell Monolayers
The objective of this study was to investigate the transepithelial transport of RVPSL (Arg-Val-Pro-Ser-Leu), an egg-white-derived peptide with angiotensin I-converting enzyme (ACE) inhibitory and antihypertensive activity, in human intestinal Caco-2 cell monolayers. Results revealed that RVPSL could be passively transported across Caco-2 cell monolayers. However, during the process of transport, 36.31% ± 1.22% of the initial RVPSL added to the apical side was degraded, but this degradation decreased to 23.49% ± 0.68% when the Caco-2 cell monolayers were preincubated with diprotin A (P < 0.001), suggesting that RVPSL had a low resistance to various brush border membrane peptidases. When transport from the apical side to the basolateral side was investigated, the apparent permeability coefficient (Papp) was (6.97 ± 1.11) × 10(-6) cm/s. The transport route of RVPSL appears to be the paracellular pathway via tight junctions, as only cytochalasin D, a disruptor of tight junctions (TJs), significantly increased the transport rate (P < 0.001). In addition, the relationship between the structure of RVPSL and transport across Caco-2 cell monolayers was studied by mutation of RVPSL. It was found that N-terminal Pro residues were more beneficial for transport of pentapeptides across Caco-2 cell monolayers than Arg and Val. Furthermore, RVPSL could be more easily transported as smaller peptides, especially in the form of dipeptides and tripeptides.
2- Zhipeng Yu et al. J. Agric. Food Chem. (2014)
Antihypertensive Effect of Angiotensin-Converting Enzyme Inhibitory Peptide RVPSL on Spontaneously Hypertensive Rats by Regulating Gene Expression of the Renin–Angiotensin System
Hen eggs are well-known for their biological functions beyond basic nutrition. In this study, the antihypertensive effect of peptide RVPSL from egg protein has been evaluated by an in vivo model. In addition, the mRNA levels of renin, AT1 receptor, angiotensin-converting enzyme (ACE), and AT2 receptor in the rat kidney were investigated through real-time polymerase chain reaction. The Ang I, Ang II, renin, and aldosterone concentrations of serum were also measured. Our results indicated that the blood pressure of the spontaneously hypertensive rats administered RVPSL for 4 weeks decreased significantly compared to that of the negative group. The mRNA levels of renin, ACE, and AT1 receptor in kidney also decreased significantly. The serum Ang II, renin, and aldosterone concentrations of the treatment group were reduced in comparison to those of the negative group. It is hoped this study will help our understanding and potential use of RVPSL in the treatment or prevention of hypertension.
3- Zhipeng Yu et al. Food & Function. (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 ((i.e., RVPSL, KLPGF, TNGIIR, and QIGLF)). 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.
4- Zhipeng Yu et al. Food Science & 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.