Serum Pro-oxidant-antioxidant Balance in Subjects with Type 2 Diabetes Mellitus.

AIM AND OBJECTIVE: Diabetes mellitus is associated with inflammation and increased oxidative stress. In the current study, we aimed to investigate the relationship between type 2 diabetes mellitus (T2DM) and serum pro-oxidant-antioxidant balance (PAB) in a large populationbased study. METHODS: In this cross-sectional study, 7888 individuals were recruited as part of the Mashhad Stroke and Heart Atherosclerotic Disorders (MASHAD) cohort study. Participants were divided into three groups based on their serum PAB values (levels < 36.4, 36.4-82.6 and > 82.6 HK). Serum PAB values were measured using a colorimetric method and enzyme-linked immune sorbent assay (ELISA). RESULTS: Serum PAB in subjects with and without diabetes was reported 76.85 ± 61.07 HK and 69.51 ± 55.50 HK. In subjects with a serum PAB > 82.6 HK the risk of T2DM was 1.2 fold higher in comparison to subjects with a serum PAB < 36.4 HK (OR: 1.26, 95% CI: 1.09 - 1.47, P-value: 0.002). This association remained significant after adjustment for confounding factors in multivariable analysis (OR: 1.19, 95% CI: 1.02 - 1.38, P-value: 0.027). CONCLUSION: Increased pro-oxidant levels may be a major complication of T2DM in our study subjects and PAB could be an indicator of higher oxidative stress in T2DM patients from northeastern Iran.

Kinetic and thermodynamic study of beta-Boswellic acid interaction with Tau protein investigated by surface plasmon resonance and molecular modeling methods.

Introduction: Beta-Boswellic acid (BBA) is a pentacyclic terpene which has been obtained from frankincense and its beneficial effects on neurodegenerative disorders such as Alzheimer's disease (AD) have been addressed. Methods: In the present study, thermodynamic and kinetic aspects of BBA interaction with Tau protein as one of the important proteins involved in AD in the absence and presence of glucose has been investigated using surface plasmon resonance (SPR) method. Tau protein was immobilized onto the carboxy methyl dextran chip and its binding interactions with BBA were studied at physiological pH at various temperatures. Glucose interference with these interactions was also investigated. Results: Results showed that BBA forms a stable complex with Tau (KD=8.45×10-7 M) at 298 K. Molecular modeling analysis showed a hydrophobic interaction between BBA and HVPGGG segment of R2 and R4 repeated domains of Tau. Conclusion: The binding affinity increased by temperature enhancement, while it decreased significantly in the presence of glucose. Both association and dissociation of the BBA-Tau complex were accompanied with an entropic activation barrier; however, positive enthalpy and entropy changes revealed that hydrophobic bonding is the main force involved in the interaction.