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The binding capacity of an antipsychotic drug, olanzapine with bovine serum albumin (BSA) was studied. The experiment was designed to investigate the interaction between olanzapine and BSA using fluorescence spectroscopy at different temperatures (298 K and 308 K). Fluorescence quenching constant was determined from Stern-Volmer equation. Van't Hoff equation was used to determine the thermodynamic parameters such as free energy (ΔG), enthalpy (ΔH) and entropy (ΔS). A strong quenching was observed in the fluorescence spectrum. The quantitative analysis revealed that olanzapine bound with BSA via a dynamic quenching through hydrophobic interactions, where binding constant K b at 280 nm was 10.28x10 4 μM -1 and 10.739x10 4 μM -1 at 298 and 308 K, whereas it was 19.31x10 4 μM -1 and 18.923x10 4 μM -1 when the study was conducted at 293 nm, respectively. The number of bound olanzapine molecules per BSA protein was ~0.5 at both the temperatures. The K b value in different temperatures suggested that the stability of BSA-olanzapine complex increased with the increase of temperature at 280 nm but reversed effect was observed in excitation wavelength of 293 nm. Positive ΔH o and ΔS o were the distinctive characteristics that allowed us to suggest that the interaction was mostly hydrophobic in nature.Citation: Rashid MA, Rabbi SNI, Sultana T, Sultan MZ, Sultan MZ (2015) Fluorescence Spectroscopic Study of Interaction between Olanzapine and Bovine Serum Albumin.

Lung cancer is one of the most frequently occurring cancers throughout the world as well as in Bangladesh. This study aimed to correlate the prognostic and/or predictive value of functional polymorphisms in SULT1A1 (rs9282861) and XRCC1 (rs25487) genes and lung cancer risk in Bangladeshi population. A case-control study was conducted which comprises 202 lung cancer patients and 242 healthy volunteers taking into account the age, sex, and smoking status. After isolation of genomic DNA, genotyping was done by polymerase chain reaction-restriction fragment length polymorphism method and the lung cancer risk was evaluated as odds ratio that was adjusted for age, sex, and smoking status. A significant association was found between SULT1A1 rs9282861 and XRCC1 rs25487 polymorphisms and lung cancer risk. In case of rs9282861 polymorphism, Arg/His (adjusted odds ratio = 5.06, 95% confidence interval = 3.05-8.41, p < 0.05) and His/His (adjusted odds ratio = 3.88, 95% confidence interval = 2.20-6.82, p < 0.05) genotypes were strongly associated with increased risk of lung cancer in comparison to the Arg/Arg genotype. In case of rs25487 polymorphism, Arg/Gln heterozygote (adjusted odds ratio = 4.57, 95% confidence interval = 2.79-7.46, p < 0.05) and Gln/Gln mutant homozygote (adjusted odds ratio = 4.99, 95% confidence interval = 2.66-9.36, p < 0.05) were also found to be significantly associated with increased risk of lung cancer. This study demonstrates that the presence of His allele and Gln allele in case of SULT1A1 rs9282861 and XRCC1 rs25487, respectively, involve in lung cancer prognosis in Bangladeshi population.

The crude methanol extract of leaves of Polygonum glabrum Willd and its Kupchan fractions were screened for cytotoxic, membrane stabilizing and thrombolytic activities. Among all fractions, the crude methanol extract showed significant cytotoxic activity having LC50 value 0.74 ± 0.045 ?g/ml. Moreover, in hypotonic solution- and heat- induced conditions, the crude methanol extract inhibited hemolysis of human erythrocyte by 79.21 ± 0.44% and 84.87±0.23%, respectively as compared to 71.9 ± 0.73% and 42.12 ± 0.37% demonstrated by the standard acetyl salicylic acid. On the other hand, in thrombolytic activity assay the methanol extract demonstrated highest clot lysis value of 35.17 ± 0.42%. DOI: http://dx.doi.org/10.3329/bpj.v17i2.22341 Bangladesh Pharmaceutical Journal 17(2): 202-204, 2014

The crude methanol extract of whole plant of Sida rhombifolia and different fractions generated from it were tested for membrane stabilizing and thrombolytic activities. In hypotonic solution-and heat-induced conditions, the chloroform soluble partitionates inhibited haemolysis of human erythrocyte by 22.11±0.14% and 64.71±0.08%, respectively as compared to 71.97±0.51% and 40.12±0.29% demonstrated by the standard acetyl salicylic acid (ASA). Moreover, the pet ether soluble materials revealed highest thrombolytic activity with clot lysis value of 19.51±0.03% as compared to 66.98±0.11% exhibited by the standard streptokinase.

Citation: Rabbi SNI, Sultan MdZ, Sohel MdD, Sultan MdZ (2015) Study of Interaction between Febuxostat and Bovine Serum Albumin by Fluorescence Spectroscopy. J Bioanal Biomed 7: 164-170. doi:10.4172/1948-593X.1000138 Copyright: © 2015 Rabbi SNI, et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. AbstractThe interaction of an anti-gout drug, febuxostat was studied with bovine serum albumin (BSA) applying fluorescence quenching method for the first time. Interaction parameter and magnitude of the force indicated for both, dynamic and static quenching in between febuxostat and BSA protein. Thermodynamic studies indicated for both hydrogen and hydrophobic interactions, observed at 280 nm and only hydrophobic at 293 nm excitation wavelength. Negative ΔH o and positive ΔS o , indicated for distinctive characteristics for the existence of both, hydrogen and hydrophobic binding throughout the interactions. The binding constant K b at λ ex =280 nm was 3.467 × 10 3 µM -1 and 4.943 × 10 3 µM -1 at 298 and 308 K temperature whereas, 5.54 × 10 3 µM -1 and 4.44 × 10 3 µM -1 was noted during excitation at λ ex =293 nm wavelength. The K b values in different temperatures assumed that the stability of binding increased with the increase of temperature at λ ex =280 nm, but reverse effect was experienced at an excitation wavelength of λ ex =293 nm. The number of bound febuxostat molecules per BSA protein was found ~1.5 at both 298 and 308 K. Study of Interaction between

IntroductionClopidogrel and aspirin are at the base of treatment in conditions like arterial thrombosis and after patients have undergone percutaneous coronary intervention. But frequently found CYP2C19*2 and CYP2C19*17 polymorphisms and some variants of the ITGB3 gene cause alteration in the therapeutic effectiveness of this drug.MethodsOne thousand cardiovascular patients were recruited for each drug under study. Their blood was collected to analyze the genotype using PCR-RFLP and T-ARMS-PCR method for clopidogrel and aspirin respectively. The PCR products for clopidogrel were screened with agarose gel electrophoresis and then digested with SmaIfor CYP2C19*2 and Nsil-HF for CYP2C19*17. The digested products of clopidogrel and the ARMS-PCR product of aspirin were run on 2% AGE to analyze the polymorphisms.ResultsIn our outcome, the percentage of hetero and mutant homozygous people in CYP2C19*2 polymorphism (loss-of-function allele) was 64.1% and for CYP2C19*17 (gain-of-function allele) was 22.3%. For ITGB3 polymorphism, it was found that 84.1% of them belonged to the homozygous group while 15.6% was heterozygous and only 0.3% were mutant homozygous patients.ConclusionOur study findings were quite compatible with the results of some other studies in other ethnic groups. This phenomenon suggested for modification of dose or application of alternative generics in patients who are under the risk of therapeutic failure or toxicity produced by these drugs.