Interaction of the Testosterone with Bovine Serum Albumin (BSA): UV-Visible Absorption Spectroscopy

The molecular interactions between BSA and Testosterone have been successfully investigated. The absorption, distribution and metabolism of many molecules can be altered based on their affinity to BSA. BSA is often increases the apparent solubility of hydrophobic ligands in plasma and modulate their delivery to cells. In this study, the interaction between Testosterone and BSA has been investigated using UV- absorption spectrophotometry and fluorescence spectroscopy to determine the binding constant. From UV- absorption spectrophotometry which showed a decreasing in the absorption intensity with increasing of the molecular ratios of testosterone to BSA, it is found that the value of the binding constant of testosterone to BSA, K equals 0.415*103 M-1 at 293 K. While from the Fluorescence spectroscopy there was a quenching in the intensity with increasing of the molecular ratios of testosterone to BSA and it gave the same value of the binding constant as uv-absorption spectroscopy.This work is supported by the German Research Foundation DFG grant no. DR228/24-

Interaction of Retinol with HSA using Spectroscopic Techniques

The interaction between retinol and HSA has been investigated using UV-absorption spectrophotometry, fluorescence spectroscopy and Fourier Transform Infrared (FT-IR) spectroscopy.UV-absorption spectrophotometry showed an increase in the absorption intensity with increasing the molecular ratios of retinol to HSA, it is found that the value of the binding constant is estimated to be1.7176×102 M-1. FTIR spectroscopy is used in the mid infrared region with Fourier self deconvolution, second derivative, difference spectra, peak picking and curve fitting were used to determine the effect of Retinol on the protein secondary structure in the amides I, II and Ill regions. Analysis of FTIR absorbance spectra is found that the intensity of the absorption bands increased with increasing the molecular ratios of retinol, however from the deconvoluted and curve fitted spectra found that the absorbance intensity for α-helix decreases relative to β-sheets, this decrease in intensity is related to the formation of H- bonding in the complex molecules

Comparative studies on the interactions between human serum albumin, bovine serum albumin and cholesterol: ftir and fluorescence spectroscopy

The interaction of the human serum albumin (HSA), bovine serum albumin (BSA) with cholesterol has been investigated. The basic binding interaction was studied by FTIR and fluorescence spectroscopy. From spectral analysis cholesterol showed a strong ability to quench the intrinsic fluorescence of HSA and BSA through a static quenching mechanism. The binding constant (k) between HSA and cholesterol is estimated to be K=2.14 × 103 M-1 at 293 K while between BSA and cholesterol is estimated to be K=.1.12 × 103 M-1 at the same temperature. FTIR spectroscopy with Fourier self-deconvolution technique was used to determine the protein secondary structure and cholesterol binding mechanisms. The observed spectral changes indicate a higher percentage of H-bonding between cholesterol and -helix compared to the percentage of H-bonding to cholesterol and -sheets.This work is supported by the German Research Foundation DFG grant No. DR228/24-

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

Analysis, characterization and some properties of polyacrylamide-Ni(II) complexes

The complexation of polyarylamide (PAam) with Ni(II) metal ions at different concentrations was investigated. The metal complexes were characterized by fourier transform infrared spectroscopy (FTIR), UV-visible, differential scanning calorimeter (DSC) and atomic force microscope (AFM). FTIR spectroscopy was used to study the characteristic shifts of the absorbance bands of C=O and N-H2. UV-visible spectroscopy was used to follow the complex formation of PAam-Ni(II) and showed the appearance of a new band that was absent both in PAam and Ni(II) salt solutions. Thermal parameters, such as the glass transition temperature (Tg) and the melting point (Tm) of the polymer-metal complex have been measured by DSC. The variation of Tg and Tm with different Ni(II) concentrations was attributed to the complexation of the native polymer during the increasing of Ni(II) concentration. AFM was used to study the surface morphology of PAam films and its complexation with Ni(II) at different concentrations. The root mean square roughness increased as the Ni(II) concentration increases

Twelve-month observational study of children with cancer in 41 countries during the COVID-19 pandemic

Introduction Childhood cancer is a leading cause of death. It is unclear whether the COVID-19 pandemic has impacted childhood cancer mortality. In this study, we aimed to establish all-cause mortality rates for childhood cancers during the COVID-19 pandemic and determine the factors associated with mortality. Methods Prospective cohort study in 109 institutions in 41 countries. Inclusion criteria: children <18 years who were newly diagnosed with or undergoing active treatment for acute lymphoblastic leukaemia, non-Hodgkin's lymphoma, Hodgkin lymphoma, retinoblastoma, Wilms tumour, glioma, osteosarcoma, Ewing sarcoma, rhabdomyosarcoma, medulloblastoma and neuroblastoma. Of 2327 cases, 2118 patients were included in the study. The primary outcome measure was all-cause mortality at 30 days, 90 days and 12 months. Results All-cause mortality was 3.4% (n=71/2084) at 30-day follow-up, 5.7% (n=113/1969) at 90-day follow-up and 13.0% (n=206/1581) at 12-month follow-up. The median time from diagnosis to multidisciplinary team (MDT) plan was longest in low-income countries (7 days, IQR 3-11). Multivariable analysis revealed several factors associated with 12-month mortality, including low-income (OR 6.99 (95% CI 2.49 to 19.68); p<0.001), lower middle income (OR 3.32 (95% CI 1.96 to 5.61); p<0.001) and upper middle income (OR 3.49 (95% CI 2.02 to 6.03); p<0.001) country status and chemotherapy (OR 0.55 (95% CI 0.36 to 0.86); p=0.008) and immunotherapy (OR 0.27 (95% CI 0.08 to 0.91); p=0.035) within 30 days from MDT plan. Multivariable analysis revealed laboratory-confirmed SARS-CoV-2 infection (OR 5.33 (95% CI 1.19 to 23.84); p=0.029) was associated with 30-day mortality. Conclusions Children with cancer are more likely to die within 30 days if infected with SARS-CoV-2. However, timely treatment reduced odds of death. This report provides crucial information to balance the benefits of providing anticancer therapy against the risks of SARS-CoV-2 infection in children with cancer

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