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

Now showing 1 - 16 of 16

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.
Biophysical Interaction of Propylthiouracil with Human and Bovine Serum Albumins
(BMC, 2019-01-30) Alsamamra, Husain; Abuteir, Musa; Darwish, Saqer
The physical interaction of antithyroid drug, propylthiouracil was studied with bovine and human serum albumins through UV absorption and fluorescence spectroscopic techniques. The obtained values of the quenching constants were calculated by the Stern-Volmer equation are in the order of 1012 Lmol-1 s-1 indicating that both serum albumins were quenched by the drug in a static manner. The binding constants of the drug interaction with both HSA and BSA proteins are found to be relatively weak and are in the order of 103 M-1. The tryptophan residues of HSA and BSA are most perturbed by the binding process which was authenticated by the fluorescence spectra of both proteins in the presence of propylthiouracil. The importance behind this study is to clarify the mechanism of the interaction between propylthiouracil with HSA and BSA, as well as providing additional values in order to study drug-protein interaction which may facilitate the study of drug metabolism and transportation.
Spectroscopic approach of the interaction study of Ceftriaxone and human serum albumin
(Academic Journals, 2013-12-10) Abu Teir, M. M.; Ghithan, J.; Abu-Taha, M. I.; Darwish, S. M.; Abu-hadid, M. M
Under physiological conditions, interaction between ceftriaxone and human serum albumin was investigated by using fluorescence spectroscopy and ultra violet (UV) absorption spectrum. From spectral analysis, ceftriaxone showed a strong ability to quench the intrinsic fluorescence of human serum albumin (HSA) through a static quenching procedure. The binding constant (k) is estimated as K=1.02× 103 M-1 at 298 K. Fourier transform infrared spectroscopy (FT-IR) spectroscopy with Fourier self-deconvolution technique was used to determine the protein secondary structure and drug binding mechanisms. The observed spectral changes indicated the formation of H-bonding between ceftriaxone and HSA molecules at higher percentage for -helix than for the -sheets.
Spectroscopic investigations of pentobarbital interaction with human serum albumin
(Elsevier, 2010-01-29) Darwish, Saqer M.; Abu sharkh, Sawsan E.; Abu Teir, Musa M.; Makharza, Sami A.; Abu-hadid, Mahmoud M.
The interaction between pentobarbital and human serum albumin has been investigated. The basic binding interaction was studied by UV-absorption and fluorescence spectroscopy. From spectral analysis pentobarbital showed a strong ability to quench the intrinsic fluorescence of HSA through a static quenching procedure. The binding constant (k) is estimated at 1.812 104 M 1 at 293 K. FT-IR spectroscopy with Fourier self-deconvolution technique was used to determine the protein secondary structure and drug binding mechanisms. The observed spectral changes of HSA–pentobarbital complex indicate a larger intensity decrease in the absorption band of a-helix relative to that of b-sheets. 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 a-helix and b-sheets.
Spectroscopic Investigations of β-Amyloid Interactions with Propofol and L-Arginine
(Scientific Research Publishing, 2015-04-29) Darwish, Saqer M.; Aiaidah, Shurook Y.; Khalid, Imtiaz M.; Abuteir, Musa M.; Qawasmi, Lena
Beta amyloid (Aβ) aggregation has been characterized to be responsible for several amyloid diseases. Fourier transform infrared (FTIR) spectroscopy, fluorescence, and atomic force microscopy (AFM) are used to investigate induced changes in the secondary structure of Aβ upon thermal denaturation and interaction with propofol and L-arginine. Spectral analysis has revealed an effective static quenching for the intrinsic fluorescence of Aβ by propofol and l-arginine with binding constants of 2.81 × 102 M−1 for Aβ-propofol and 0.37 × 102 M−1 for Aβ-L-arginine. Fourier self-deconvolution (FSD) technique has been used to evaluate the relative intensity changes in the spectra of the component bands in the amide I and amide II regions at different ligand’s concentration in the protein complex. The analysis showed a decrease in the intensities of the parallel beta bands of propofol and L-arginine interactions with Aβ, accompanied with an increase in the antiparallel bands for the Aβ-propofol interaction and a decrease for the Aβ-l-arginine interaction. The relative increase in peaks’ intensities at 1694 cm−1 and 1531 cm−1 for the propofol interaction is linked to the formation of oligomers in the protein.
Spectroscopic study of propofol binding to human serum albumin
(World Scientific, 2010-11-10) Darwish, Saqer M.
The interaction of propofol and human serum albumin (HSA) has been investigated by UV-absorption, fluorescence spectroscopy and Fourier transform infrared (FT-IR) spectroscopy. Propofol has shown a strong ability to quench the intrinsic fluorescence of HSA through a static quenching procedure. The binding constant (k) is estimated at a low value of 2.55×103 M−1 at 293K. FT-IR spectroscopy with Fourier self-deconvolution technique was used to determine the protein secondary structure in the amide regions I, II and III. The observed spectral changes of HSA-propofol complex indicate a larger intensity decrease in the absorption band of α-helix relative to that of β-sheets. 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.
Study of Progesterone interaction with Human Serum Albumin: Spectroscopic approach
(2011-01-17) Abu Teir, M. M.; Ghithan, J. H.; Darwish, S. M.; Abu-Hadid, M. M.
The interaction between progesterone and human serum albumin has been investigated. This interaction was studied by UV-absorption and fluorescence spectroscopy. From spectral analysis progesterone showed a strong ability to quench the intrinsic fluorescence of HSA through a static quenching procedure. The binding constant (K) is estimated 6.56×102 M-1 at 293 K. FT-IR spectroscopy with Fourier self-deconvolution technique was used to determine HSA secondary structure and progesterone binding mechanisms. The observed spectral changes indicate the formation of H-bonding between progesterone and HSA molecules which can be related to the intensity decrease in the absorption band of α-helix relative to that of β-sheets.
Study the interaction of hydrophobic vitamins (vitamin E and vitamin D) with HSA using Spectroscopic techniques
(Quality Scientific Publishing, 2014-06-25) Abu Teir, M. M; Abu Awwad, I.; Abu-Hadid, M. M.; Darwish, S. M.
The interaction of hydrophobic vitamins (vitamin E and vitamin D) 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 vitamins (vitamin E and vitamin D) with HSA has been investigated by using UV-absorption, and Fourier transforms infrared (FT-IR) spectroscopy. The binding constants of vitamin E and vitamin D have been determined by UV-absorption. The values of the binding constants are calculated at room temperature: (1.21×102M-1) and (6.8×101M-1) for vitamin E- HSA and vitamin D- HSA mixtures, respectively. 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 vitamins 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.
تأثير تفاعل المصل البقري مع ذرات النانو من الذهب
(AL-Quds University, 2018-01-13) اشرف كامل جواعدة; Ashraf kamel jawadeh; موسى ابو طير; Dr. Husain Alsamamra; Salman M Salman; Mustafa Abu Safa
دراسة المطيافية لتفاعل فيتامين k1 مع بروتين بلازما دم الإنسان 'الألبومين' HSA
(AL-Quds University, 2013-02-24) علا فهد جميل حوراني; Ola Fahid Jameel Hoorani; موسى أبو طير; د. محمود أبو حديد; د. خولة قمحية; د. جمال غبون
دراسة تأثير البروبوفول و الأرجنين على البيتا أميلويد بواسطة تقنيات مطيافية الجزيئات
(AL-Quds University, 2014-02-01) شروق يوسف محمد عيايده; Shurook Yousef Mohammad Ayaydeh; صقر درويش; د. موسى ابو طير; جمال غضمون
دراسة تأثير التستوستيرون على الالبومبيه البروتيه النبقل في بلازمب الذم بواسطة تقنيبت مطيبفة الجسيئبت
(AL-Quds University, 2014-05-10) روان محمد خالد القواسمه; rawan mohammad khalid alqawasma; موسى أبو طير; د. محمود أبو حديد; No
دراسة تأثير الديجوتنين على احد انواع الدهون المكونة للخلية ((SOPC بواسطة تقنيات مطيافة الجزيئات.
(AL-Quds University, 2017-12-09) ابراهيم غازي موسى هوارين; ibrahim ghaze mosa hawwarin; موسى أبو طير; Dr. Husain Samamra; Dr. Lelia Mashal
دراسة تأثير رتينول على الالبوماين البروتين الناقل في بلازما الدم بواسطة تقنيات مطيافة الجزيئات
(AL-Quds University, 2017-12-23) رزق سلمان حماد درابيع; riziq salman hammad drabee; موسى أبو سير; Husain Alsamamra; Jamal Ghabbon
دراسة تفاعل الفيتامينات المحبة للماء (فيتامين ج و فيتامين ب 12) مع مصل البيومين البشري باستخدام التقنيات المطيافية
(AL-Quds University, 2018-04-15) محمد ايمن محمد ابو علان; Mohammad Ayman Mohammad Abuallan; حسين السمامرة; Musa Abutier; Jamal Ghabboun
دراسة عينات بيولوجية باستخدام الأشعة تحت الحمراء
(AL-Quds University, 2017-12-20) اية علي ابراهيم ذويب; thweib ibrahim ali Aya; رشدي كتانه; Prof. Mohammad Abu Taha; Amin Leghrouz; Hisham Hidmi

Musa Abuteir

Sawsan Abusharkh

Saqer Darwish

Husain Alsamamra

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