Hyperglycemia induced structural and functional changes in human serum albumin of diabetic patients: a physico-chemical study

2016 ◽  
Vol 12 (8) ◽  
pp. 2481-2489 ◽  
Author(s):  
Km Neelofar ◽  
Zarina Arif ◽  
Khursheed Alam ◽  
Jamal Ahmad
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Significant Role ◽  
Chemical Study ◽  
Diabetic Patients ◽  
Kidney Dysfunction ◽  
Functional Changes ◽  
Physico Chemical ◽  
Diabetes Progression

Structural and functional changes in glycated-HSA, isolated from diabetic patients, suggests it has a significant role in diabetes progression and kidney dysfunction.

The transfer of glyburide across human placenta obtained from healthy and diabetic patients and the role of human serum albumin

2005 ◽  
Vol 193 (6) ◽  
pp. S92
Author(s):  
Ilona Nekhayeva ◽  
Tatiana Nanovskaya ◽  
Gary Hankins ◽  
Natasha Dziuba ◽  
Mahmoud Ahmed
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Human Placenta ◽  
Diabetic Patients

scholarly journals Mechanism of interaction of hypoglycemic agents glimepiride and glipizide with human serum albumin

2009 ◽  
Vol 7 (1) ◽  
pp. 96-104 ◽  
Author(s):  
Neelam Seedher ◽  
Mamta Kanojia
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Conformational Changes ◽  
Hydrophobic Interactions ◽  
Drug Binding ◽  
Hypoglycemic Agents ◽  
Diabetic Patients ◽  
Quenching Mechanism ◽  
Mechanism Of Interaction

AbstractThe mechanism of interaction of hypoglycemic drugs, glimepiride and glipizide with human serum albumin (HSA) has been studied using fluorescence spectroscopy. The results are discussed in terms of the binding parameters, thermodynamics of the binding process, nature of forces involved in the interaction, identification of drug binding site on serum albumin and the fluorescence quenching mechanism involved. The association constants were of the order of 105 and glipizide was found to have much higher affinity for HSA than glimepiride at all temperatures. Thermodynamic parameters for the binding suggested that hydrophobic interactions are primarily involved in the binding of these drugs to HSA. However, glimepiride and glipizide appear to cause temperature-dependent conformational changes in the albumin molecule and, therefore, the nature of interaction varied with temperature. Glimepiride and glipizide bind to both site I and site II on HSA, but the primary interaction occurs at site II. The binding region in site II is different for the two drugs. Stern-Volmer analysis of quenching data indicated that tryptophan residues of HSA are not fully accessible to the drugs and a predominantly dynamic quenching mechanism is involved in the binding. Results can provide useful insight into prediction of competitive displacement of these drugs by other co-administered drugs and excipients, resulting in serious fluctuations of the blood glucose levels in diabetic patients.

scholarly journals Structural and functional changes of oxidized human serum albumin: Physiological and pathological significance for hepatic biomarker.

2008 ◽  
Vol 52 (2) ◽  
pp. 25-30
Author(s):  
Naoyuki Yamada ◽  
Kazuyuki Kubota ◽  
Asami Kawakami ◽  
Akira Nakayama ◽  
Ei-Ichiro Suzuki
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Functional Changes

Pancreatic Bile-Salt-Dependent Lipase Activity in Serum of Diabetic Patients: Is There a Relationship with Glycation?

1998 ◽  
Vol 94 (2) ◽  
pp. 181-188 ◽  
Author(s):  
Nathalie Caillol ◽  
Eric Pasqualini ◽  
Eric Mas ◽  
Régis Guieu ◽  
Anne Valette ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Bile Salt ◽  
Human Serum ◽  
Lipase Activity ◽  
Specific Activity ◽  
Density Lipoprotein ◽  
Diabetic Patients

1. Pancreatic bile-salt-dependent lipase has been detected in human plasma where it has the capability to modify normal low- and high-density lipoprotein composition and structure and to reduce the atherogenicity of oxidized low-density lipoprotein (Shamir R, Johnson WJ, Morlock-Fitzpatrick K, Zolfaghari R, Li L, Mas E, Lombardo D, Morel DW, Fisher EA. Pancreatic carboxyl ester lipase: a circulating enzyme that modifies normal and oxidized lipoproteins in vitro. J Clin Invest 1996; 97: 1696–704). 2. In the present study, we investigated the effect of glycation and particularly that of human serum albumin on the activity of bile-salt-dependent lipase. In vitro, bile-salt-dependent lipase activity decreased in the presence of human serum albumin; however, this was less pronounced in the presence of glycated human serum albumin. In vivo, bile-salt-dependent lipase specific activity was about 2-fold higher in the sera of diabetic patients than in the sera of normal subjects. 3. A significant increase in the specific activity of bile-salt-dependent lipase related to the serum level of glycation was observed. The increase in bile-salt-dependent lipase specific activity was not related to the glucose concentration in serum suggesting that glycation of bile-salt-dependent lipase could not be involved in the observed effects. Although the stability of serum bile-salt-dependent lipase was important enough to allow a systemic action of the enzyme on lipoproteins, it could not explain the higher activity of the enzyme in diabetic serum. 4. We concluded that bile-salt-dependent lipase could be helpful against the premature development of atherosclerosis in diabetes.

scholarly journals Hydroxyurea-Loaded Albumin Nanoparticles: Preparation, Characterization, and In Vitro Studies

Pharmaceutics ◽  
2019 ◽  
Vol 11 (8) ◽  
pp. 410 ◽  
Author(s):  
Tazhbayev ◽  
Mukashev ◽  
Burkeev ◽  
Kreuter
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Crosslinking Agent ◽  
Drug Carriers ◽  
Potential Yield ◽  
Albumin Nanoparticles ◽  
Natural Agents ◽  
Physico Chemical

Human serum albumin nanoparticles (HSA-NPs) have been widely used as drug delivery systems. In most cases, HSA-NPs are formed by the method of desolvation in the presence of glutaraldehyde as a crosslinking agent. In the present study, we showed the possibility of crosslinking human serum albumin (HSA) molecules with natural agents, urea, and cysteine at the nanoparticle level under mild conditions (at room temperature of 20–25 °C). Optimal concentrations of the interacting components (HSA, urea, and cysteine) were found to produce nanoparticles with optimal physico-chemical parameters (particle size, polydispersity, zeta potential, yield, etc.) for application as drug carriers. We used hydroxyurea (HU), a simple organic compound currently used as a cancer chemotherapeutic agent. The results indicated sizes of 196 ± 5 nm and 288 ± 10 nm with a surface charge of −22 ± 3.4 mV and −17.4 ± 0.5 mV for HSA-NPs (20 mg/mL of HSA, 0.01 mg/mL of cysteine, and 10 mg/mL of urea) and HSA–HU-NPs (2 mg/mL of HU), respectively. The yield of the HSA–HU-NPs was ~93% with an encapsulation efficiency of ~77%. Thus, the particles created (immobilized with HU) were stable over time and able to prolong the effect of the drug.

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