By table of contents Book description Spectroscopy and Modeling of Biomolecular Building Blocks presents an overview of recent advances in the intertwining of the following research fields: The coupling of these disciplines offers a new point of view to the understanding of isolated elementary building blocks of biomolecules and their assemblies. It allows the unambiguous separation between intrinsic properties of biomolecular systems and those induced by the presence of their environment. The first chapters provide background in modelling Ifrequency-resolved spectroscopy using microwave, infrared and UV photons, time-resolved spectroscopy in the femtosecond domain and energy-resolved electron spectroscopy II and production of gas-phase neutral and ionic biomolecular species, mass-spectrometry, ion mobility and BIRD techniques III.
The results of synchronous? The simultaneous presence of LMF and COL in binding to HSA should be taken into account in the multidrug therapy, and necessity of using a monitoring therapy owning to the possible increase of the uncontrolled toxic effects. Introduction Human serum albumin HSA is the most abundant carrier protein in blood circulation that can bind many endogenous and exogenous compounds e.
The structure of HSA has been determined crystallographically [2,3] and discovered that it consisted of three structurally homologous, predominantly helical domains domain I, II and IIIwhich each domain contained two subdomains A and B.
The drugs bound in site I are generally bulky heterocyclic anions with the charge situated in a central position of the molecules and that in site II are aromatic carboxylic acids with n Corresponding author.
HSA is a globular protein composed of a single polypeptide chain of amino acid residues with a Spectroscopy and modeling alpha-helical structure. Its amino acid sequence contains a total of 17 disul? It Spectroscopy and modeling capable of binding a wide variety of drugs and xenobiotics [6—11].
Binding of drugs to plasma proteins is an important pharmacological parameter, since it frequently affects the distribution and elimination of a drug as well as the duration and intensity of its physiological action [12—14].
Drugs, which are administered in multi-drug therapy, may alter each others binding to the transporting protein. Therefore, it is necessary to determine both the location of the binding sites and the possible interactions for each individual drug.
Combination of several drugs is often required, especially during long-term therapy. The simultaneous presence of two drugs for the binding sites on HSA may result in decrease in binding and hence increase in the concentration of free biologically active fraction of one or both the drugs.
Therefore, study of the interaction between HSA and drugs is imperative and can obtain a lot of information of drug actions. Colchicine produces its antiin? The effects of drugs on the HSA are estimated and the binding constant, the number of binding sites and protein conformational changes of drug-HSA complexes are determined.
A dilution series of drugs were prepared in a 50 mM phosphate buffer. For each data point, 5 ml of the drug solution was added into 2 ml HSA solution. The reaction time has been investigated and the results showed that 3 min was enough for the stabilization.
So the change in? The addition of a constant volume of quencher to the protein solution avoided complications due to dilution effects within titration type experiments.
Each measurement was repeated in triplicate and the mean and standard deviation were calculated. By scanning both the excitation and emission monochromators of a common spectro? All RLS spectra were obtained by scanning simultaneously the excitation and emission monochromators namely Dl?
Circular dichroism measurements Circular dichroism CD measurements were carried out on a Jasco automatic recording spectropolarimeter Japan in cell of path length 2 mm at room temperature.
The induced ellipticity was obtained by the ellipticity of the drug-HSA mixture subtracting the ellipticity of drug at the same wavelength and is expressed in degrees.
The results are expressed as mean residue ellipticity MRE in deg. The yobs represents the CD in milli-degree, n is the number of amino acid residuesl and Cp are the path length of the cell and the mole fraction, respectively.
The complexes Colchicine, Lome? All compounds were energy minimized by means of AM1 semi-empirical force? The energy minimized ligands were further processed using Autodock tools program, adding partial atomic charges for each atom, and de?
A grid map for the whole protein structure?
Materials and methods 2. All reagents were used as supplied without further puri? The protein was dissolved in 50 mM phosphate buffer solutions at pH 7. All other reagents were of analytical grade and doubly distilled water used through out all the experiments.
Fluorescence measurements Fluorescence spectra were recorded at room temperature with a Eclips carry?
The sigmoidal distance-dependent the electric permittivity of Mehler and Solmajer was used for the calculation of the electrostatic grid maps. The lamarkian genetic algorithm method was applied for minimization, using default parameters and random starting positions on the entire protein area, random orientations and torsions were used for ligands.
After determining high af? Results and discussion 3. When the excitation wavelength is nm, only the tryptophan residue has a? At the excitation wavelength of nm, both tryptophan and tyrosyl amino acid residues have?Spectroscopy welcomes manuscripts that describe techniques and applications of all forms of spectroscopy and that are of immediate interest to users in industry, academia, and government.
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