The role of parenting styles on effort perseverance: the mediating role of conscientiousness and mindfulness

The present study investigates the role of parenting styles on effort perseverance with mediating roles of conscientiousness and mindfulness as moderators. For this purpose, 272 Iranian high school girl students were chosen by stratified random sampling. Data were analyzed by Path Analysis and Hierarchical Regression methods. The results showed that maternal control, parental control and maternal responsibility predict effort perseverance through conscientiousness; and paternal responsibility indicates positive and significant relationship with effort perseverance. Furthermore, findings showed that the relationship between conscientiousness and effort perseverance was moderated by mindfulness. Parenting style is an important factor in predicting effort perseverance through conscientiousness. In addition, being mindfulness has an effective role in relation to conscientiousness and effort perseverance

Matrix augmentation as an efficient method for resolving interaction of bromocriptine with human serum albumin: trouble shooting and simultaneous resolution

This work reports the results of an interesting study related to the investigation of interactions of bromocriptine (BCP) with human serum albumin (HSA) by mathematicall modelling of voltammetric and spectroscopic data into an augmented data matrix and its resolution by multivariate curve resolution-alternating least squares (MCR-ALS). The quality of the results obtained by MCR-ALS was examined by MCR-BANDS and its outputs confirmed the absence of rotational ambiguities in the MCR-ALS results. BCP-HSA interactions were also modeled by molecular docking methods to verify the results obtained from experimental sections and fortunately, they were compatible. Hard modeling of the experimental data by EQUISPEC helped us to calculate the binding constant of the complex formed from BCP-HSA interactions which was in a good agreement with that of calculated from direct analysis of the experimental data. Finally, with the help of two different amperometric measurements based on BCP-HSA interactions a novel electroanalytical method was developed for biosensing of HSA in serum samples.Fil: Jalalvand, Ali R.. Kermanshah University of Medical Sciences; IránFil: Ghobadi, Sirous. Kermanshah University of Medical Sciences; IránFil: Goicoechea, Hector Casimiro. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe; Argentina. Universidad Nacional del Litoral. Facultad de Bioquímica y Ciencias Biológicas. Laboratorio de Desarrollo Analítico y Quimiometría; ArgentinaFil: Faramarzi, Elahe. Kermanshah University of Medical Sciences; IránFil: Mahmoudi, Majid. Kermanshah University of Medical Sciences; Irá

Mathematical modeling of interactions of cabergoline with human serum albumin for biosensing of human serum albumin

In this work, we are going to study the interactions of cabergoline (CBG) with human serum albumin (HSA) by mathematical modeling of voltammetric and spectroscopic data. To achieve this goal, voltammetric and spectroscopic data will be augmented into a data matrix which will be resolved by multivariate curve resolution-alternating least squares (MCR-ALS) as a powerful chemometric tool. Then, the quality of the data fitting by MCR-ALS will be examined by MCR-BANDS to ensure about the absence of the rotational ambiguities in the results. Molecular docking will also be used to model the interactions of CBG with HSA for verifying the results obtained from experimental methods. Hard-modeling of the experimental data will be performed by EQUISPEC to compute the binding constant of the complex formed from the interactions of CBG with HSA for verifying the binding constant obtained by direct analysis of the experimental data. Finally, two chrono-amperometric measurements based on CBG-HSA interactions will be performed to develop a novel electroanalytical method for determination of electro-inactive HSA.Fil: Jalalvand, Ali R.. Kermanshah University of Medical Sciences; IránFil: Ghobadi, Sirous. Razi University; IránFil: Akbari, Vali. Razi University; Irán. Kermanshah University of Medical Sciences; IránFil: Goicoechea, Hector Casimiro. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe; Argentina. Universidad Nacional del Litoral. Facultad de Bioquímica y Ciencias Biológicas. Laboratorio de Desarrollo Analítico y Quimiometría; ArgentinaFil: Faramarzi, Elahe. Kermanshah University of Medical Sciences; IránFil: Mahmoudi, Majid. Kermanshah University of Medical Sciences; Irá

Multiple Solutions for a p (x)-Laplacian Problem: A Variational Approach

We focus on an anisotropic p (x)-Laplacian equation defined on a bounded domain with smooth boundary. Moreover, using variational methods to find the existence of at least three solutions due to Ricceri is discussed

Investigation of interactions of Comtan with human serum albumin by mathematically modeled voltammetric data: A study from bio-interaction to biosensing

In this work, voltammetric data recorded at a glassy carbon electrode (GCE) were separately used to investigate the interactions of entacapone (Comtan, CAT) with human serum albumin (HSA). Then, an augmented data matrix was constructed by the combination of voltammetric and spectroscopic data and simultaneously analysed by multivariate curve resolution-alternating least squares (MCR-ALS) to obtain more information about CAT-HSA interactions. The absence of rotational ambiguities in results obtained by MCR-ALS was verified with the help of MCR-BANDS and we confirmed that the results were unambiguous and reliable. Binding of CAT to HSA was also modeled by molecular docking and the results were compatible with those of obtained by recording experimental data. Hard-modeling of combined voltammetric and spectroscopic data by EQUISPEC as an efficient chemometric algorithm helped us to compute binding constant of CAT-HSA complex specie which was in a good agreement with the binding constant value obtained by direct analysis of experimental data. For electrochemical sensing of serum albumin two amperometric measurements were performed to determine HSA in 2–27 nM and 27–70 nM with a limit of detection of 0.51 nM and a sensitivity of 1.84 μA nM−1.Fil: Jalalvand, Ali R.. Kermanshah University of Medical Sciences; IránFil: Ghobadi, Sirous. Razi University; IránFil: Goicoechea, Hector Casimiro. Universidad Nacional del Litoral; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe; ArgentinaFil: Gu, Hui Wen. Yangtze University; ChinaFil: Sanchooli, Esmael. University of Zabol; Irá

Chemometrics-assisted investigation of interactions of Tasmar with human serum albumin at a glassy carbon disk: Application to electrochemical biosensing of electro-inactive serum albumin

In this work, voltammetric data recorded by a glassy carbon electrode (GCE) was used to investigate the interactions of tolcapone (Tasmar, TAS) with human serum albumin (HSA) at the electrode surface. The recorded voltammetric data was also combined with spectroscopic data to construct an augmented data matrix which was analysed by multivariate curve resolution-alternating least squares (MCR-ALS) as an efficient chemometric tool to obtain more information about TAS-HSA interactions. The results of MCR-ALS confirmed formation of one complex species (HSA-TAS2) and application of MCR-BANDS to the results of MCR-ALS confirmed the absence of rotational ambiguities and existing unambiguous and reliable results. Binding of TAS to HSA was also modeled by molecular docking and the results showed that the TAS was bound to sub-domain IIA of HSA which were compatible with the ones obtained by recording experimental data. Hard-modeling of combined voltammetric and spectroscopic data by EQUISPEC helped us to compute binding constant of HSA-TAS2 complex species which was compatible with the binding constant value obtained by direct analysis of experimental data. Finally, a new electroanalytical method was developed based on TAS-HSA interactions for determination of HSA in two ranges of 0–541 nM and 541–1200 nM with a limit of detection of 0.04 nM and a sensitivity of 0.02 μA nM−1.Fil: Mohammadi, Ghobad. Kermanshah University of Medical Sciences; IránFil: Faramarzi, Elahe. Kermanshah University of Medical Sciences; IránFil: Mahmoudi, Majid. Kermanshah University of Medical Sciences; IránFil: Ghobadi, Sirous. Razi University; IránFil: Ghiasvand, Ali Reza. Lorestan University; IránFil: Goicoechea, Hector Casimiro. Universidad Nacional del Litoral; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe; ArgentinaFil: Jalalvand, Ali R.. Kermanshah University of Medical Sciences; Irá

Two-and three-way chemometric analyses for investigation of interactions of acarbose with normal and glycated human serum albumin: developing a novel biosensing system

In this project, our research group has performed an interesting work in which interactions of acarbose (ACB) with normal human serum albumin (HSA) and glycated HSA (GHSA) have been investigated by chemometrics assisted-electrochemical and spectroscopic techniques. To have a deep insight to the interactions of ACB with HSA and GHSA, different electrochemical and spectroscopic techniques were used to monitor ACB-HSA and ACB-GHSA interactions and analyzed by multivariate curve resolution alternating least squares (MCR-ALS), MCR-BANNDS and EQUISPEC as efficient chemometric algorithms. Then, molecular docking techniques were used to extract more information which helped us to better justify binding of ACB with HSA and GHSA. After obtaining qualitative and quantitative information and justification of the ACB-HSA and ACB-GHSA interactions, a novel electrochemical technique was developed for exploiting second-order advantage from differential pulse voltammetric data for determination of GHSA as a potential biomarker in diabetes in the presence of HSA. Calibration and validation of the developed system showed us that our system was successful in determination of GHSA in synthetic and real samples.Fil: Nazari, Maryam. Razi University; Irán. Tehran University of Medical Sciences; IránFil: Kashanian, Soheila. Razi University; IránFil: Omidfar, Kobra. Tehran University of Medical Sciences; IránFil: Ghobadi, Sirous. Razi University; IránFil: Goicoechea, Hector Casimiro. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe; Argentina. Universidad Nacional del Litoral. Facultad de Bioquímica y Ciencias Biológicas. Laboratorio de Desarrollo Analítico y Quimiometría; ArgentinaFil: Gu, Hui Wen. Yangtze University; ChinaFil: Khodarahmi, Reza. Kermanshah University of Medical Sciences; IránFil: Jalalvand, Ali R.. Kermanshah University Of Medical Sciences; Irá

Fabrication of a novel naltrexone biosensor based on a computationally engineered nanobiocomposite

A computationally engineered impedimetric naltrexone (NLT) biosensor based on immobilization of bovine serum albumin (BSA) onto fullerene-C60/glassy carbon electrode (FLR/GCE) has been developed using initial characterization by computational methods and complementing them by experimental ones. Computational results showed that BSA hydrophobically binds to FLR which is energetically favorable and leads to the spontaneous formation of the stable nanobiocomposite and also showed that interaction of NLT with BSA is mainly driven by hydrogen bonding and hydrophobic interactions. Besides complementing the computational studies, experimental results showed that addition of FLR to the surface of the electrode facilitated electron transfer reactions, and also showed that the presence of BSA inhibits the interfacial electron transfer in some extent due to the nonconductive properties of BSA. The presence of NLT may form a negatively charged electroactive complex with BSA which repels the negatively charged redox probe and decelerates interfacial electron transfer leading to obvious faradaic impedance change. The faradaic impedance responses were linearly related to naltrexone concentration between 0.1 nM and 80 nM and limit of detection (LOD) was calculated to be 0.01 nM (3Sb/b). Finally, the proposed biosensor was successfully applied to determination of NLT in urine samples of both healthy and addict volunteers.Fil: Gholivand, Mohammad Bagher. Razi University. Faculty of Chemistry; IránFil: Jalalvand, Ali R.. Razi University. Faculty of Chemistry; Irán. Universidad Nacional del Litoral; ArgentinaFil: Paimard, Giti. Razi University. Faculty of Chemistry; IránFil: Goicoechea, Hector Casimiro. Universidad Nacional del Litoral; ArgentinaFil: Skov, Thomas. Universidad de Copenhagen; DinamarcaFil: Farhadi, Reza. Razi University. Faculty of Chemistry; IránFil: Ghobadi, Sirous. Razi University. Faculty of Science. Department of Biology; IránFil: Moradi, Nozar. Razi University. Faculty of Chemistry; IránFil: Nasirian, Vahid. Razi University. Faculty of Chemistry; Irá