Buy Procyanidin B2
The purpose of procyanidin encapsulation is to stabilize and reduce premature oxidation of the product. Apple exact and procyanidin are water-soluble. SalSphere technology allows for transformation of the water-soluble potent ingredients into hydrophobic submicron spheres that are suspendable and can penetrate the hair follicles due to their size and hydrophobic nature. The submicron spheres encapsulate the procyanidin B2 and release their content over time at the hair roots for effective and targeted delivery.
buy procyanidin b2
The functional ingredient is procyanidin B2 oligomer, a natural source of polyphenols that belong to the class of bioflavonoids, catechin. This compound is found in the skins of unripe green apples. Clinical studies at the Tsukuba Research Laboratories in Japan have shown that topical application of procyanidin B2 improves hair growth and hair diameter.
In clinical studies, 71% of subjects showed an increased number of hairs, and 78.9% showed an increased mean value of hair diameter. The results identified procyanidin B2 from apples to be a powerful stimulant that promotes hair epithelial cell growth more than 300% relative to controls at a concentration of 30 μM.
Although this form of application was found successful, the therapy requires 6 months of daily application to see results, which is considered as a long time for most consumers. In addition, the attempt to utilize pure procyanidin in commercial application did not show expected results due to three major reasons: 1. The high solubility of procyanidin B2 in water at pH 7.2 is approximately 10 mg/ml which makes it easy to get rinsed off. 2. Procyanidin is not adhering nor penetrating into the follicles efficiently, and 3. Procyanidin tends to get oxidized in a short time changing the color to dark brown. Encapsulation of procyanidin into submicron sphere found to be the ultimate solution to enable successful commercial use.
SalSphere technology effectively shields procyanidin B2 from oxidative forces and maintains the aesthetics and potency in final product formulations. Free procyanidin B2 turns dark brown in a formula whereas a product using SalSphere remains lighter in color.
The diameter of a hair follicle orifice is estimated to be in the range of 30-50 μm. The SalSphere delivery system, with a diameter of 0.1-0.3 μm, can facilitate penetration of procyanidin B2 into the hair follicle in a targeted manner increasing the efficacy.
Utilizing fluorescent agents encapsulated in SalSphere demonstrated the targeted delivery of the submicron spheres containing the active to the hair follicles. The targeted delivery of procyanidin B2 can specifically promote hair epithelial cell growth, activate specific regions of the hair follicle into the growing phase, and cause the follicular hair cycle to revert to the anagen phase from the telogen phase. Thus, it is suggested to be effective in curing male pattern baldness.
Effects of procyanidin B2 on body composition. A: Weight gain curves; B: Total weight gain; C: Food intake curves; D: Liver index. The data are expressed as means SD. aP
Effects of procyanidin B2 on serum lipid profile, insulin resistance, and endotoxemia. Serum triglycerides (A), total cholesterol (B), low-density lipoprotein cholesterol (C), high-density lipoprotein cholesterol (D) and fasting glucose (E), fasting insulin (F) and the intravenous glucose tolerance test (G), units of area under the curve (H) and lipopolysaccharides (I). The data are expressed as means SD. aP
Effects of procyanidin B2 on hepatic steatosis. A: Hematoxylin and eosin staining of liver in CHOW group, HCD group and procyanidin B2 group; B: Liver weight; C: Alanine transaminase; D: Aspartate transaminase; E: Relative expression levels of steroid response element binding protein 1c; F: Relative expression levels of fatty acid synthase; G: Relative expression levels of carnitine palmitoyltransferase. The data are expressed as means SD. aP
Effects of procyanidin B2 on gut microbiota. A: Principal coordinate analysis of the gut microbiota based on unweighted UniFrac distances between groups; B: Relative abundance of gut microbiota in phylum; C: Venn diagrams described the number of operational taxonomic units that are distinct and shared across the groups; D: Heatmap: Community hierarchical clustering analysis of major taxonomic groups at genus level, the red represents high relative abundance and the blue represent low relative abundance; E: Relative abundance of gut microbiota in genus. HCD: High-fat-cholesterol diet; PB2: Procyanidin B2; PCoA: Principal coordinate analysis; OTUs: Operational taxonomic units.
Procyanidins are the flavanols from polyphenols commonly found in fruits and red wine. Recent studies have shown that procyanidins possess potential anti-inflammatory activities. However, underlying mechanisms remain to be understood. Inflammasomes are multi-protein complexes composed of pro-caspase and pattern recognition receptors (PRRs) such as NOD-like receptor family, pyrin domain containing 3 (NLRP3). Since aberrant activation of NLRP3 inflammasome is implicated in the pathogeneses of pro-inflammatory diseases such as diabetes, atherosclerosis and arthritis, we aimed to investigate whether procyanidin B2 (PCB2), the most widely distributed natural procyanidins, inhibits the activation of NLRP3 inflammasome in endothelial cells (ECs). We found that, in human umbilical vein ECs (HUVECs), PCB2 significantly suppressed the activation of NLRP3 inflammasome and inhibited subsequent caspase-1 activation and interleukin (IL)-1β secretion in response to lipopolysaccharides (LPS). PCB2 negatively regulated the gene expression of NLRP3. In addition, PCB2 attenuated LPS-induced production of reactive oxygen species (ROS) and the transcriptional activity of activator protein-1 (AP-1). In conclusion, we demonstrated for the first time that procyanidin B2 inhibits NLRP3 inflammasome activation via suppression of AP-1 pathway in ECs. These results suggest a new mechanism by which natural flavoids such as procyanidins exert their vascular protective effects.
DNA methyltransferases (DNMTs) is a key epigenetic enzyme for pharmacological manipulation and is employed in cancer reprogramming. During past few years multiple strategies have been implemented to excavate epigenetic compounds targeting DNMTs. In light of the emerging concept of chemoinformatics, molecular docking and simulation studies have been employed to accelerate the development of DNMT inhibitors. Among the DNMT inhibitors known till date, epigallocathechin-3-gallate (EGCG) was identified to be effective in reducing DNMT activity. However, the broad spectrum of EGCG to other diseases and variable target enzymes offers some limitations. In view of this, 32 EGCG analogues were screened at S-Adnosyl-L-homocysteine (SAH) binding pocket of DNMTs and procyanidin B2-3, 3'-di-O-gallate (procyanidin B2) was obtained as potent inhibitor having medicinally relevant chemical space. Further, in vitro analysis demonstrates the efficiency of procyanidin B2 in attenuating DNMT activity at IC50 of 6.880.647 μM and subsequently enhancing the expression of DNMT target genes, E-cadherin, Maspin and BRCA1. Moreover, the toxic property of procyanidin B2 towards triple negative breast cancer cells to normal cells offers platform for pre-clinical trial and an insight to the treatment of cancer.
Apoptosis is a critical event in the pathogenesis of lung ischemia/reperfusion (I/R) injury. Sirtuin 3 (SIRT3), an important deacetylase predominantly localized in mitochondria, regulates diverse physiological processes, including apoptosis. However, the detailed mechanisms by which SIRT3 regulates lung I/R injury remain unclear. Many polyphenols strongly regulate the sirtuin family. In this study, we found that a polyphenol compound, procyanidin B2 (PCB2), activated SIRT3 in mouse lungs. Due to this effect, PCB2 administration attenuated histological lesions, relieved pulmonary dysfunction, and improved the survival rate of the murine model of lung I/R injury. Additionally, this treatment inhibited hypoxia/reoxygenation (H/R)-induced A549 cell apoptosis and rescued Bcl-2 expression. Using Sirt3-knockout mice and specific SIRT3 knockdown in vitro, we further found that SIRT3 strongly protects against lung I/R injury. Sirt3 deficiency or enzymatic inactivation substantially aggravated lung I/R-induced pulmonary lesions, promoted apoptosis, and abolished PCB2-mediated protection. Mitochondrial pyruvate kinase M2 (PKM2) inhibits apoptosis by stabilizing Bcl-2. Here, we found that PKM2 accumulates and is hyperacetylated in mitochondria upon lung I/R injury. By screening the potential sites of PKM2 acetylation, we found that SIRT3 deacetylates the K433 residue of PKM2 in A549 cells. Transfection with a deacetylated mimic plasmid of PKM2 noticeably reduced apoptosis, while acetylated mimic transfection abolished the protective effect of PKM2. Furthermore, PKM2 knockdown or inhibition in vivo significantly abrogated the antiapoptotic effects of SIRT3 upregulation. Collectively, this study provides the first evidence that the SIRT3/PKM2 pathway is a protective target for the suppression of apoptosis in lung I/R injury. Moreover, this study identifies K433 deacetylation of PKM2 as a novel modification that regulates its anti-apoptotic activity. In addition, PCB2-mediated modulation of the SIRT3/PKM2 pathway may significantly protect against lung I/R injury, suggesting a novel prophylactic strategy for lung I/R injury. 041b061a72