Spectroscopic approach of the interaction study of Ceftriaxone and human serum albumin
| dc.contributor.author | Abu Teir, M. M. | |
| dc.contributor.author | Ghithan, J. | |
| dc.contributor.author | Abu-Taha, M. I. | |
| dc.contributor.author | Darwish, S. M. | |
| dc.contributor.author | Abu-hadid, M. M | |
| dc.date.accessioned | 2018-09-10T17:59:30Z | |
| dc.date.available | 2018-09-10T17:59:30Z | |
| dc.date.issued | 2013-12-10 | |
| dc.description.abstract | 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. | en_US |
| dc.description.sponsorship | This work was supported by the German Research Foundation DFG Grant No. DR228/24-2. | en_US |
| dc.identifier.issn | 2141-2200 | |
| dc.identifier.uri | https://dspace.alquds.edu/handle/20.500.12213/883 | |
| dc.language.iso | en_US | en_US |
| dc.publisher | Academic Journals | en_US |
| dc.subject | Ceftriaxone | en_US |
| dc.subject | amide I-III | en_US |
| dc.subject | binding mode | en_US |
| dc.subject | binding constant | en_US |
| dc.subject | protein secondary structure | en_US |
| dc.subject | Fourier transform IR | en_US |
| dc.subject | UV-spectroscopy | en_US |
| dc.subject | Flurosence spectroscopy | en_US |
| dc.title | Spectroscopic approach of the interaction study of Ceftriaxone and human serum albumin | en_US |
| dc.type | Article | en_US |