- Tytuł:
- Evaluation of p-phenylene-bis and phenyl dithiocarbamate sodium salts as inhibitors of mushroom tyrosinase
- Autorzy:
-
Amin, Ehsan
Saboury, Ali
Mansouri-Torshizi, Hassan
Zolghadri, Samane
Bordbar, Abdol-Khalegh - Powiązania:
- https://bibliotekanauki.pl/articles/1040368.pdf
- Data publikacji:
- 2010
- Wydawca:
- Polskie Towarzystwo Biochemiczne
- Tematy:
-
phenyl dithiocarbamate
mushroom tyrosinase
mixed inhibition
p-phenylene-bis (dithiocarbamate)
noncompetitive inhibition
inhibition constant - Opis:
- Two structurally related compounds, phenyl dithiocarbamate sodium salt (I) and p-phenylene-bis (dithiocarbamate) sodium salt (II) were prepared by reaction of the parent aniline and p-phenylenediamine with CS2 in the presence of sodium hydroxide. These water soluble compounds were characterized by spectroscopic techniques, IR, 1H NMR and elemental analysis. The inhibitory effects of both compounds on both activities of mushroom tyrosinase (MT) from Agricus bisporus were studied at two temperatures, 27°C and 37°C. L-3, 4-dihydroxyphenylalanine (L-DOPA), and l-tyrosine were used as natural substrates for the catecholase and cresolase enzyme reactions, respectively. Kinetic analysis confirmed noncompetitive inhibition mode of I and mixed type of II on both activities of MT; I and II inhibit MT with inhibition constants (KI) of 300 µM and 4 µM, respectively. Analysis of thermodynamic parameters indicated predominant involvement of hydrophobic interactions in binding of I and electrostatic ones in binding of II to MT. It seems that II is a more potent MT inhibitor due to its two charged head groups able to chelate copper ions in the enzyme active site. Intrinsic fluorescence studies as a function of concentrations of both compounds showed unexpectedly quenching of emission intensity without any shift of emission maximum. Extrinsic ANS-fluorescence indicated that only binding of I induces limited changes in the tertiary structure of MT, in agreement with the postulated hydrophobic nature of the binding mechanism.
- Źródło:
-
Acta Biochimica Polonica; 2010, 57, 3; 277-283
0001-527X - Pojawia się w:
- Acta Biochimica Polonica
- Dostawca treści:
- Biblioteka Nauki
Artykuł