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    Wyświetlanie 1-4 z 4
    Tytuł:
    Inhibition study of adenosine deaminase by caffeine using spectroscopy and isothermal titration calorimetry.
    Autorzy:
    Saboury, A
    Divsalar, A
    Ataie, G
    Amanlou, M
    Moosavi-Movahedi, A
    Hakimelahi, G
    Powiązania:
    https://bibliotekanauki.pl/articles/1043464.pdf
    Data publikacji:
    2003
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    calorimetry
    inhibition
    caffeine
    adenosine deaminase
    Opis:
    Kinetic and thermodynamic studies were made on the effect of caffeine on the activity of adenosine deaminase in 50 mM sodium phosphate buffer, pH 7.5, using UV spectrophotometry and isothermal titration calorimetry (ITC). An uncompetitive inhibition was observed for caffeine. A graphical fitting method was used for determination of binding constant and enthalpy of inhibitor binding by using isothermal titration microcalorimetry data. The dissociation-binding constant is equal to 350 μM by the microcalorimetry method, which agrees well with the value of 342 μM for the inhibition constant that was obtained from the spectroscopy method. Positive dependence of caffeine binding on temperature indicates a hydrophobic interaction.
    Źródło:
    Acta Biochimica Polonica; 2003, 50, 3; 849-855
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Thermodynamics of specific protein-RNA interactions.
    Autorzy:
    Stolarski, Ryszard
    Powiązania:
    https://bibliotekanauki.pl/articles/1043600.pdf
    Data publikacji:
    2003
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    calorimetry
    thermodynamics
    fluorescence
    proteins
    specific binding
    RNA 5' cap
    Opis:
    Description of the recognition specificity between proteins and nucleic acids at the level of molecular interactions is one of the most challenging tasks in biophysics. It is key to understanding the course and control of gene expression and to the application of the thus acquired knowledge in chemotherapy. This review presents experimental results of thermodynamic studies and a discussion of the role of thermodynamics in formation and stability of functional protein-RNA complexes, with a special attention to the interactions involving mRNA 5' cap and cap-binding proteins in the initiation of protein biosynthesis in the eukaryotic cell. A theoretical framework for analysis of the thermodynamic parameters of protein-nucleic acid association is also briefly surveyed. Overshadowed by more spectacular achievements in structural studies, the thermodynamic investigations are of equal importance for full comprehension of biopolymers' activity in a quantitative way. In this regard, thermodynamics gives a direct insight into the energetic and entropic characteristics of complex macromolecular systems in their natural environment, aqueous solution, and thus complements the structural view derived from X-ray crystallography and multidimensional NMR. Further development of the thermodynamic approach toward interpretation of recognition and binding specificity in terms of molecular biophysics requires more profound contribution from statistical mechanics.
    Źródło:
    Acta Biochimica Polonica; 2003, 50, 2; 297-318
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Structure-function relationship of serine protease-protein inhibitor interaction.
    Autorzy:
    Otlewski, Jacek
    Jaskólski, Mariusz
    Buczek, Olga
    Cierpicki, Tomasz
    Czapińska, Honorata
    Krowarsch, Daniel
    Smalas, Arne
    Stachowiak, Damian
    Szpineta, Agnieszka
    Dadlez, Michał
    Powiązania:
    https://bibliotekanauki.pl/articles/1044133.pdf
    Data publikacji:
    2001
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    calorimetry
    serine proteases
    structural thermodynamics
    protein inhibitor
    protein-protein recognition
    Opis:
    We report our progress in understanding the structure-function relationship of the interaction between protein inhibitors and several serine proteases. Recently, we have determined high resolution solution structures of two inhibitors Apis mellifera chymotrypsin inhibitor-1 (AMCI-I) and Linum usitatissimum trypsin inhibitor (LUTI) in the free state and an ultra high resolution X-ray structure of BPTI. All three inhibitors, despite totally different scaffolds, contain a solvent exposed loop of similar conformation which is highly complementary to the enzyme active site. Isothermal calorimetry data show that the interaction between wild type BPTI and chymotrypsin is entropy driven and that the enthalpy component opposes complex formation. Our research is focused on extensive mutagenesis of the four positions from the protease binding loop of BPTI: P1, P1', P3, and P4. We mutated these residues to different amino acids and the variants were characterized by determination of the association constants, stability parameters and crystal structures of protease-inhibitor complexes. Accommodation of the P1 residue in the S1 pocket of four proteases: chymotrypsin, trypsin, neutrophil elastase and cathepsin G was probed with 18 P1 variants. High resolution X-ray structures of ten complexes between bovine trypsin and P1 variants of BPTI have been determined and compared with the cognate P1 Lys side chain. Mutations of the wild type Ala16 (P1') to larger side chains always caused a drop of the association constant. According to the crystal structure of the Leu16 BPTI-trypsin complex, introduction of the larger residue at the P1' position leads to steric conflicts in the vicinity of the mutation. Finally, mutations at the P4 site allowed an improvement of the association with several serine proteases involved in blood clotting. Conversely, introduction of Ser, Val, and Phe in place of Gly12 (P4) had invariably a destabilizing effect on the complex with these proteases.
    Źródło:
    Acta Biochimica Polonica; 2001, 48, 2; 419-428
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    The interaction of new oxicam derivatives with lipid bilayers as measured by calorimetry and fluorescence spectroscopy
    Autorzy:
    Maniewska, Jadwiga
    Gąsiorowska, Justyna
    Szczęśniak-Sięga, Berenika
    Michalak, Krystyna
    Powiązania:
    https://bibliotekanauki.pl/articles/1038386.pdf
    Data publikacji:
    2018
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    oxicam derivatives
    NSAIDs analogues
    piroxicam
    1,2- benzothiazine derivatives synthesis
    model lipid bilayers
    differential scanning calorimetry (DSC)
    fluorescence spectroscopy
    Opis:
    The purpose of the present work was to assess the ability of five new oxicam analogues to interact with the lipid bilayers. To characterize the interaction of newly synthesized NSAIDs (non-steroidal anti-inflammatory drugs) analogues with DPPC lipid bilayers the two following techniques were applied - differential scanning calorimetry (DSC) and fluorescence spectroscopy. The results obtained by these experimental approaches show that new oxicams analogues interact with the lipid model membranes under consideration. As demonstrated both in calorimetric and spectroscopic studies, the greatest influence on the thermotropic properties of the lipid membrane and on the quenching of fluorescence of Laurdan and Prodan was exerted by a derivative named PR47 containing in its structure a two-carbon aliphatic linker with a carbonyl group, as well as bromine and trifluoromethyl substituents.
    Źródło:
    Acta Biochimica Polonica; 2018, 65, 2; 185-191
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
      Wyświetlanie 1-4 z 4

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