Uncovering the Effects of Alcohol on Green Tea Polyphenols Release from Albumin Nanoparticles - Cytology and Genetics

Abstract Alcohol-induced dose dumping is a major concern in modified-release formulations. We developed green tea polyphenols encapsulated albumin nanoparticles (GTP-ALB-NPs) to check the key factors governing alcohol-induced dose dumping. GTP-ALB-NPs were prepared from 10% albumin solution and 5mg/mL GTP. Nanoparticles were characterized by dynamic light scattering (DLS), atomic force microscopy (AFM), and high-resolution scanning electron microscopy (HR-SEM). Drug solubility, swelling behavior, media uptake, and wettability/contact angle measurement were studied. In vitro drug release was studied in release medium with different quantities of alcohol and release kinetics was determined. The similarity factor (f2) test was used to assess the dissolving characteristics of the drug in both alcoholic and non-alcoholic media and the corresponding change in the medium was calculated. GTP-ALB-NPs of <100 nm size were synthesized. GTP became more soluble when the amount of alcohol in the release media was increased. Similar results were witnessed for swelling behavior and the media uptake studies. Contact angle measurements showed all dissolution profiles to be < 90°. The cumulative release of GTP was increased with the increase of alcohol in the release medium. Maximum GTP release (~95%) was observed in PBS with 40% alcohol in 48 h, showing no dose dumping. The release data followed an anomalous mode of drug dissolution and were modeled into zero-order kinetics. The six months stability testing conducted at 25 ± 2°C revealed no significant difference. GTP-ALB-NPs showed a positive effect in alcoholic media compared to nonalcoholic medium. Increased alcohol proportion increased along with the drug release percentage. GTP-ALB-NPs could be safe for alcohol-induced dose dumping and used as a potent carrier of GTP.

SpringerLink

💡 Our scientists discovered a new infection strategy in #Candida albicans: human #albumin reprograms its metabolism, turning harmless strains pathogenic – without the need of hyphae or toxins.
#NatCommun #LeibnizHKI

🗞️ Read our press release: https://lmy.de/mthFi or the
🧪 original publication in Nature Communications: https://rdcu.be/exl7d

@dfg_public

article from 2022:

Albumin Binds COVID-19 Spike 1 Subunit and Predicts In-Hospital Survival of Infected Patients—Possible Alteration by Glucose
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8836760/

#albumin #SpikeProtein #covid

Albumin Binds COVID-19 Spike 1 Subunit and Predicts In-Hospital Survival of Infected Patients—Possible Alteration by Glucose

(1) Background: This study aimed to analyze if the serum albumin levels of hospitalized SARS-CoV-2 (COVID-19) patients on admission could predict <30 days in-hospital all-cause mortality, and if glucose levels on admission affected this predictive ...

PubMed Central (PMC)

related, from 2012:

Serum albumin prevents protein aggregation and amyloid formation and retains chaperone-like activity in the presence of physiological ligands
https://pubmed.ncbi.nlm.nih.gov/22549788/

"Although serum albumin has an established function as a transport protein, evidence is emerging that serum albumin may also have a role as a molecular chaperone. Using established techniques to characterize chaperone interactions, this study demonstrates that bovine serum albumin: 1) preferentially binds stressed over unstressed client proteins; 2) forms stable, soluble, high molecular weight complexes with stressed client proteins; 3) reduces the aggregation of client proteins when it is present at physiological levels; and 4) inhibits amyloid formation by both WT and L55P transthyretin. Although the antiaggregatory effect of serum albumin is maintained in the presence of physiological levels of Ca(2+) and Cu(2+), the presence of free fatty acids significantly alters this activity: stabilizing serum albumin at normal levels but diminishing chaperone-like activity at high concentrations. Moreover, here it is shown that depletion of albumin from human plasma leads to a significant increase in aggregation under physiologically relevant heat and shear stresses. This study demonstrates that serum albumin possesses chaperone-like properties and that this activity is maintained under a number of physiologically relevant conditions."

#albumin #amyloid

Serum albumin prevents protein aggregation and amyloid formation and retains chaperone-like activity in the presence of physiological ligands - PubMed

Although serum albumin has an established function as a transport protein, evidence is emerging that serum albumin may also have a role as a molecular chaperone. Using established techniques to characterize chaperone interactions, this study demonstrates that bovine serum albumin: 1) preferentially …

PubMed

research article from 2011:

Loss of functional albumin triggers acceleration of transthyretin amyloid fibril formation in familial amyloidotic polyneuropathy
https://www.nature.com/articles/labinvest201171

"Human serum albumin, the most abundant protein in plasma, serves as a transporter of various ligands and an antioxidant in blood circulation. Human serum albumin is a mixture of a reduced form (human mercaptalbumin: HMA) and an oxidized form (human nonmercaptalbumin: HNA). Albumin is the major antioxidant in plasma, and a large proportion of all the serum antioxidant properties can be attributed to albumin. Previous work has shown the total reactive antioxidant potential in plasma, considered as an index of the level of antioxidants, decreased in patients with FAP. In addition, more recent work demonstrated that albumin suppressed amyloid formation of amyloid-β(Aβ), a component of amyloid fibrils in Alzheimer's disease, by reducing oxidative stress. These data suggest that albumin functing as an antioxidant may perform a crucial role in amyloid formation in FAP."

#amyloidosis #albumin #OxidativeStress

Loss of functional albumin triggers acceleration of transthyretin amyloid fibril formation in familial amyloidotic polyneuropathy - Laboratory Investigation

Transthyretin (TTR)-related familial amyloidotic polyneuropathy (FAP) is characterized by systemic accumulation of amyloid fibrils caused by a point mutation in the TTR gene. Despite the urgent need for alternative therapeutic strategies, the pathogenesis of FAP still remains elusive. In our study reported here, we focused on albumin, the most abundant protein in plasma, and described the role of albumin in the TTR amyloid-formation process. Patients with FAP evidenced significantly decreased serum albumin levels as the disease progressed. Biacore analysis showed that albumin had a binding affinity for TTR and exhibited higher affinity for TTR amyloid than native TTR. Albumin functioning as an antioxidant effectively suppressed TTR amyloid formation. In patients with FAP, albumin was significantly oxidized as the disease progressed. Moreover, loss of functional albumin accelerated TTR deposition in analbuminemic rats possessing a human variant TTR gene. Taken together, these results indicate that albumin may have an inhibitory role in the TTR amyloid-formation process.

Nature
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I found that this #egg for #breakfast was cracked and in fact #frozen. So, after carefully removing the #shell, you can see the #yolk through the clear #albumin. Still, it made a good #omelette eventually.

#MyWork #MyPhoto #CCBYSA #Android

Albumin’: David Holmes Presents The Free Association

New year, new thing to try for maybe a few days! I realized with my recent Apple Music year in review (no Spotify, sorry but I like having a music library, I’ll keep reveling in my vestigial millen…

Dot Matrix with Stereo Sound

@rombarthelemy @BakkeHK Sorry, that was just a general comment on the psychological effect, not trying to argue against #albumin; quite the opposite!

Very interesting article and thank you for sharing it! Do you have any thoughts on timing and benefit, purely in terms of #glycocalyx damage?

Is the benefit of albumin constant regardless of the degree of existing glycocalyx damage? Or is there a point where, if the disruption is severe enough, it stops being effective?

@razvan @BakkeHK Not at all. The purpose of using #albumin in #SepticShock is precisely to prevent or mitigate #glycocalyx damage. If oncontic pressure gradient was the purpose, any synthetic colloid would do the job (actually, they won’t, because of the altered endothelial layer, as you suggested)

https://annalsofintensivecare.springeropen.com/articles/10.1186/s13613-020-00697-1

https://link.springer.com/article/10.1007/s00134-022-06740-y

Role of albumin in the preservation of endothelial glycocalyx integrity and the microcirculation: a review - Annals of Intensive Care

The endothelial glycocalyx comprises a complex layer of membrane-bound proteoglycans, secreted glycosaminoglycans, glycoproteins, glycolipids and bound plasma proteins such as albumin and antithrombin associated with the endothelial surface. The glycocalyx plays an important role in vascular homeostasis, regulating vascular permeability and cell adhesion, and acts as a mechanosensor for hemodynamic shear stresses; it also has antithrombotic and anti-inflammatory functions. Plasma proteins such as albumin are physiologically bound within the glycocalyx, thus contributing to stability of the layer. Albumin is the major determinant of plasma colloid osmotic pressure. In addition, albumin transports sphingosine-1-phosphate which has protective endothelial effects, acts as a free radical scavenger, and has immunomodulatory and anti-inflammatory effects. This review examines the physiological function of the endothelial glycocalyx and the role of human albumin in preserving glycocalyx integrity and the microcirculation.

SpringerOpen