Biophysics Research Laboratory

Permanent URI for this collection

http://dspace.alquds.edu:4000/handle/20.500.12213/135

Overview

The biophysics lab has been established at Al-Quds University in 2005 with a generous fund from the DFG of the Federal Republic of Germany. The lab has supported several research students in the fields of physics and biology; several of whom are currently finishing their Doctorates degrees in Germany and the U.S. The research lab provides services to students and faculty members in the physics, biology, chemistry, and environmental science programs, in addition to an open cooperation with the college of medicine, pharmacy and the Nanotechnology center.

Our Team

    • Musa Abuteir

    Ph.D Physics / Director

    • Sawsan Abusharkh

    Ph.D. Biomedical physics

    Saqer Darwish

    Ph.D Physics

    Husain Alsamamra

    Ph.D Physics

    Research Topics

    • Study of the interactions between different proteins (such as transthyretin, beta amyloid, Bovine Serum Albumin and Human serum albumin) and a variety of drugs and ligands such as pentobarbital, propofol, arginine, Procaine, Dopamine cholesterols and vitamins.

    • Design and develop drug delivery systems that could transport anti-cancer drugs to site of interest .

    • Synthesis and Characterization of nanoparticle drug delivery systems for different purposes.

    Browse

    Browsing Biophysics Research Laboratory by Author "Abu Teir, Musa M"

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      Binding of Vitamin K1(Phylloquinone) to Human Serum Albumin(HSA):Spectroscopic studies
      (Dr.V.K.Sharma, 2014-09-07) Abu Teir, Musa M; Hourani, Ola; Darwish, Saker M; Abu-hadid, Mahmoud M
      The interaction of hydrophobic vitamin (vitamin K1) with human serum albumin (HSA) at physiological (pH 6.9- 7.4) has been studied using UV-VIS spectrometer, and an FT-IR spectroscopy. The interaction of hydrophobic vitamin (vitamin K1) with HSA has been investigated by using UV-absorption, and Fourier transforms infrared (FT-IR) spectroscopy. The binding constant of vitamin K1 has been determined by UV-absorption. The value of the binding constant for vitamin K1 -HSA is calculated at room temperature 293 K and it was determined as 60 M����. FT-IR spectroscopy with Fourier self- deconvolution technique and second derivative resolution enhancement procedures were applied in the analysis of the amide I, amid II, and amid III regions to determine the protein secondary structure and hydrophobic vitamin binding mechanisms. All peaks positions in the three amide regions (amid I, amide II and amide III) have been assigned and any changes due to concentration changes have been investigated. The FTIR spectra measurements indicate a change in the intensity of absorption bands due to change in the concentrations in drugs. In addition a larger intensity decrease in the absorption band of α-helix relative to that of β-sheets has been observed. This variation in intensity is related indirectly to the formation of H-bonding in the complex molecules, which accounts for the different intrinsic propensities of α-helix and β-sheets.