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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.
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.
Genetic, serological and biochemical characterization of Leishmania tropica fromfoci in northern Palestine and discovery of zymodeme MON-307
(Springer, 2012-06-18) Abdelmajeed Nasseraldeen; Kefaya Azmi; Schnur, Lionel; Pratlong, Francine; Baidouri, Fouad; Ravel, Christophe; Dedet, Jean-Pierre; Ereqat, Suheir; Abdeen, Ziad; Schonian, Gabriele
Background: Many cases of cutaneous leishmaniasis (CL) have been recorded in the Jenin District based on their clinical appearance. Here, their parasites have been characterized in depth. Methods: Leishmanial parasites isolated from 12 human cases of CL from the Jenin District were cultured as promastigotes, whose DNA was extracted. The ITS1 sequence and the 7SL RNA gene were analysed as was the kinetoplast minicircle DNA (kDNA) sequence. Excreted factor (EF) serotyping and multilocus enzyme electrophoresis (MLEE) were also applied. Results: This extensive characterization identified the strains as Leishmania tropica of two very distinct sub-types that parallel the two sub-groups discerned by multilocus microsatellite typing (MLMT) done previously. A high degree of congruity was displayed among the results generated by the different analytical methods that had examined various cellular components and exposed intra-specific heterogeneity among the 12 strains. Three of the ten strains subjected to MLEE constituted a new zymodeme, zymodeme MON-307, and seven belonged to the known zymodeme MON-137. Ten of the 15 enzymes in the profile of zymodeme MON-307 displayed different electrophoretic mobilities compared with the enzyme profile of the zymodeme MON-137. The closest profile to that of zymodeme MON-307 was that of the zymodeme MON-76 known from Syria. Strains of the zymodeme MON-307 were EF sub-serotype A2 and those of the zymodeme MON-137 were either A9 or A9B4. The sub-serotype B4 component appears, so far, to be unique to some strains of L. tropica of zymodeme MON-137. Strains of the zymodeme MON-137 displayed a distinctive fragment of 417 bp that was absent in those of zymodeme MON-307 when their kDNA was digested with the endonuclease RsaI. kDNA-RFLP after digestion with the endonuclease MboI facilitated a further level of differentiation that partially coincided with the geographical distribution of the human cases from which the strains came. Conclusions: The Palestinian strains that were assigned to different genetic groups differed in their MLEE profiles and their EF types. A new zymodeme, zymodeme MON-307 was discovered that seems to be unique to the northern part of the Palestinian West Bank. What seemed to be a straight forward classical situation of L. tropica causing anthroponotic CL in the Jenin District might be a more complex situation, owing to the presence of two separate sub-types of L. tropica that, possibly, indicates two separate transmission cycles involving two separate types of phlebotomine sand fly vector.
Increased Prevalence of Human Cutaneous Leishmaniasis in Israel and The Palestinian Authority Caused by the Recent Emergence of a Population of Genetically Similar Strains of Leishmania tropica
(Elsevier, 2016-08-05) Azmi, Kifaya; Krayter, Lena; Nasereddin, Abedelmajeed; Ereqat, Suheir; Schnur, Lionel; Al-Jawabreh, Amer; Abdeen, Ziad; Schonian, Gabriele
Twelve unlinked microsatellite markers were used to determine the microsatellite profiles of 50 newly and 46 previously typed strains of L. tropica from various Israeli and Palestinian foci. Their microsatellite profiles were compared to those of 99 previously typed strains of L. tropica from 15 countries. Israeli and Palestinian strains of L. tropica fell into three different groups, one of which contained 75 of the 96 Israeli and Palestinian strains. This population separated fromall the others at the first hierarchical level by Bayesian statistics and formed a distinct monophyletic group on applying genetic distance and allele frequency analyses. The second cluster contained ten Israeli strains from a specific focus north of the Sea of Galilee,whichwere previously shown to differ from all other strains of L. tropica in their serological, biochemical and molecular biological parameters. This clusterwas closely related to clusters comprising strains of L. tropica from Africa. Four Israeli and five Palestinian strains fell into different genetic entities mostly related to strains from Asian foci of CL. Importation during numerous migrations of humans and, perhaps, infected reservoir animals in the past and, now, through modern travel is the most likely explanation for the existence of so many locally encountered genetic variants of L. tropica in the Israeli-Palestinian region. Geographical and ecological variation may play a role in expanding the genetic heterogeneity once given importations had become established in different foci. Currently, one population is expanding in the area comprising almost all of the Palestinian and Israeli strains of L. tropica isolated since 1996 and investigated in this study, which differ clearly from all other strains ofwhatsoever origin. This population seems to result from the re-emergence of a previously existing genotype owing to environmental changes and human activities.
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

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