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  1. Roslan AA, Tayyab S
    Biochem Mol Biol Educ, 2019 03;47(2):156-160.
    PMID: 30629781 DOI: 10.1002/bmb.21207
    A laboratory exercise on the interaction between the herbicide pendimethalin (PM) and goat serum albumin (GSA), a carrier protein present in mammalian blood circulation, is described. Fluorescence spectroscopy was used to study the binding reaction between PM and GSA. Titration of a constant amount of the protein (GSA) with increasing ligand (PM) concentrations produced a consecutive decrease in the protein's fluorescence. Treatment of the fluorescence quenching data according to the Stern-Volmer equation yielded the values of the Stern-Volmer constant (Ksv ) and bimolecular quenching rate constant (kq ), whereas values of the binding constant (Ka ) and number of binding sites (n) were obtained from the double logarithmic plot. This experiment provides an exciting opportunity for undergraduate students to independently perform ligand binding studies with a protein, in addition to providing the means for the determination of their binding parameters. © 2019 International Union of Biochemistry and Molecular Biology, 47(2): 156-160, 2019.
  2. Roslan AA, Rahman NA, Alam MK
    J Orthod Sci, 2018;7:16.
    PMID: 30271761 DOI: 10.4103/jos.JOS_37_18
    OBJECTIVE: This study was carried to study the prevalence of dental anomalies and treatment modalities/planning among the orthodontic patients.

    MATERIALS AND METHODS: A total of 370 orthodontic records including their pre-treatment orthopantomographs (OPG) and study models of orthodontic patients in permanent dentition who attended dental clinic were assessed for impaction, hypodontia, supernumerary, supraocclusion, infraocclusion, and any other anomalies excluding the third molars. The association of anomalies with gender status and racial status was analyzed using Pearson's Chi-square test. A P value of <0.05 is considered as significant. The confidence interval at 95% (CI) was set.

    RESULTS: Among the 370 subjects, 105 (28.4%) presented with at least one anomaly. Eighty-five (23%) demonstrated a single anomaly and 20 (5.4%) with more than one anomaly. The most prevalent anomaly was impaction (14.32%), followed by hypodontia (7.03%). The less common anomalies were microdontia (1.08%), dilacerations (0.27%), and generalised enamel hypoplasia (0.27%). Maxillary right lateral incisors and canines were the most common affected teeth and these are located on the maxillary right quadrant. It was evident that dental anomalies were statistically dependant on race (P = 0.025), but independent of gender. The most common treatment planned for these patients was fixed appliance.

    CONCLUSIONS: Impaction was predominant among 28.4% subjects observed with anomaly and most patients with anomaly are treated with fixed appliances (49%).

    CLINICAL RELEVANCE: These anomalies play a great role in occlusion and alignment in treatment planning and relapse for orthodontic treatment.

  3. Kabir MZ, Roslan AA, Ridzwan NFW, Mohamad SB, Tayyab S
    J Biomol Struct Dyn, 2020 Jun;38(9):2693-2703.
    PMID: 31271347 DOI: 10.1080/07391102.2019.1640133
    Molecular interaction of the 3,4-methylenedioxy-β-nitrostyrene (MNS), an inhibitor of platelet aggregation with the main transport protein, albumin from human serum (HSA) was explored using absorption, fluorescence and circular dichroism (CD) spectroscopy in combination with in silico analyses. The MNS-HSA complexation was corroborated from the fluorescence and absorption spectral results. Implication of static quenching mechanism for MNS-HSA system was predicted from the Stern-Volmer constant, KSV-temperature relationship as well as the bimolecular quenching rate constant, kq values. Stabilization of the complex was affirmed by the value of the binding constant (Ka = 0.56-1.48 × 104 M-1). Thermodynamic data revealed that the MNS-HSA association was spontaneously driven mainly through hydrophobic interactions along with van der Waal's interaction and H-bonds. These results were well supported by in silico interpretations. Far-UV and near-UV CD spectral results manifested small variations in the protein's secondary and tertiary structures, respectively, while three-dimensional fluorescence spectra displayed microenvironmental fluctuations around protein's fluorophores, upon MNS binding. Significant improvement in the protein's thermostability was evident from the temperature-stability results of MNS-bound HSA. Binding locus of MNS, as identified by competitive drug displacement findings as well as in silico analysis, was found to be located in subdomain IIA (Sudlow's site I) of the protein.Communicated by Ramaswamy H. Sarma.
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