Spectroscopic approach of the interaction study of Ceftriaxone and human serum albumin

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.This work was supported by the German Research Foundation DFG Grant No. DR228/24-2

Spectroscopic investigations of pentobarbital interaction with human serum albumin

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.This work is supported by the German Research Foundation DFG Grant No. DR228/24-2

A Deterministic Algorithm for Arabic Character Recognition Based on Letter Properties

Handheld devices are flooding the market, and their use is becoming essential among people. Hence, the need for fast and accurate character recognition methods that ease the data entry process for users arises. There are many methods developed for handwriting character recognition especially for Latin-based languages. On the other hand, character recognition methods for Arabic language are lacking and rare. The Arabic language has many traits that differentiate it from other languages: first, the writing process is from right to left; second, the letter changes shape according to the position in the work; and third, the writing is cursive. Such traits compel to produce a special character recognition method that helps in producing applications for Arabic language. This research proposes a deterministic algorithm that recognizes Arabic alphabet letters. The algorithm is based on four categorizations of Arabic alphabet letters. Then, the research suggested a deterministic algorithm composed of 34 rules that can predict the character based on the use of all of categorizations as attributes assembled in a matrix for this purpose

Lean service, business strategy and ABC and their impact on firm performance

This is an Accepted Manuscript of an article published by Taylor & Francis in Production Planning & Control on 14 May 2019, available online: https://www.tandfonline.com/doi/full/10.1080/09537287.2019.159914

Study the interaction of hydrophobic vitamins (vitamin E and vitamin D) with HSA using Spectroscopic techniques

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.This work is supported by the German Research Foundation DFG Grant No. DR228/24-2