MINT MINT, Dpt of Biology, University of Rome Tor Vergata MINT http://mint.bio.uniroma2.it/mint url>http://mint.bio.uniroma2.it/mint/ https://mint.bio.uniroma2.it MINT-[0-9]+ https://mint.bio.uniroma2.it/index.php/results-interactions/?id=${ac} The Molecular INTeraction database (MINT) is a relational database designed to store interactions between biological molecules. http://mint.bio.uniroma2.it Inhibition of amyloid fibrillation of lysozyme by phenolic compounds involves quinoprotein formation. Inhibition of amyloid fibrillation of lysozyme by phenolic compounds involves quinoprotein formation. FEBS Lett. (0014-5793) 2012 Feng S., Song XH., Zeng CM. in vitro In vitro tem transmission electron microscopy tem predetermined predetermined participant predetermined Feng S., Song XH., Zeng CM. FEBS Lett. (0014-5793) 2012 Inhibition of amyloid fibrillation of lysozyme by phenolic compounds involves quinoprotein formation. Inhibition of amyloid fibrillation of lysozyme by phenolic compounds involves quinoprotein formation. FEBS Lett. (0014-5793) 2012 Feng S., Song XH., Zeng CM. in vitro In vitro fluorescence fluorescence technology fluorescence predetermined predetermined participant predetermined Feng S., Song XH., Zeng CM. FEBS Lett. (0014-5793) 2012 lysc_chick Lysozyme C LYZ 1,4-beta-N-acetylmuramidase C Allergen Gal d IV protein protein chick Gallus gallus (Chicken) Chicken MRSLLILVLCFLPLAALGKVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAKFESNFNTQATNRNTDGSTDYGILQINSRWWCNDGRTPGSRNLCNIPCSALLSSDITASVNCAKKIVSDGNGMNAWVAWRNRCKGTDVQAWIRGCRL DIP protein P00698 original sequence version: 158 81E85743FF579468 lyz-lyz 2 Lysozyme 3 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified Lysozyme 3 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified direct interaction direct interaction f2 homomint mint ThT is a fluorescent probe for monitoring the formation and growth of amyloid fibrils. The fluorescence intensity of ThT increased significantly when the compound specifically binding to the highly ordered β-sheet structure of amyloid fibrils [14]. As depicted in Fig. 2A, an increase in ThT fluorescence emission was observed after incubating the control sample for 3 days. The intensity of ThT fluorescence increased gradually as the amyloid formation progressed until reached to a plateau after 12 days of incubation. In the presence of phenol or resorcinol (100 μg/mL), the ThT profiles showed similar pattern as that of the control experiment, indicating that these two compounds had no effect on lysozyme fibrillation. In contrast, the o- and p-isomers of diphenol, catechol and hydroquinone, exhibited inhibitory effects on amyloid formation of lysozyme in a dose-dependent fashion. For instance, co-incubation of lysozyme with 25, 50 and 100 μg/mL of catechol resulted in a reduction in ThT fluorescence of mature fibrils 21.2%, 33.3% and 68.9%, respectively (Fig. 2B). lyz-lyz-1 1 Lysozyme 3 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified Lysozyme 3 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified direct interaction direct interaction f3 homomint mint The inhibitory effects of catechol and hydroquinone on lysozyme fibrillation were supported by TEM determination of the fibrils. Fig. 3A-E shows the TEM images of lysozyme assemblies aged 12 days prepared in the presence or absence of phenols. In 106 the absence of a phenolic compound, the matured lysozyme fibrils showed a typical 107 amyloid morphology, characterized as long, straight and dense fibrils with diameters of 8 30 nm (Fig. 3A). In the presence of phenol (Fig. 3B) and resorcinol (Fig. 3C), the lysozyme fibrils showed similar morphologies to the control fibrils. In contrast, incubation of lysozyme with 110 catechol or hydroquinone resulted in a noticeable reduction of amyloid fibrils. The resultant fibrils coexisted with amorphous particles and a few beads-on-string protofibrils [6,15], as shown in Fig. 3D and E.