MINT MINT, Dpt of Biology, University of Rome Tor Vergata MINT http://mint.bio.uniroma2.it/mint url&gt;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 and disaggregation of α-synuclein oligomers by natural polyphenolic compounds. Inhibition and disaggregation of α-synuclein oligomers by natural polyphenolic compounds. FEBS Lett. (0014-5793) 2011 imex curation Caruana M., Högen T., Levin J., Hillmer A., Giese A., Vassallo N. SIFT (Scanning for Intensely Fluorescent Targets) has been used. Only protein-protein interactions in vitro In vitro biophysical biophysical tag fluorescence tag visualisation by fluorescence tag fluorescence Caruana M., Högen T., Levin J., Hillmer A., Giese A., Vassallo N. SIFT (Scanning for Intensely Fluorescent Targets) has been used. FEBS Lett. (0014-5793) 2011 Only protein-protein interactions imex curation syua_human Alpha-synuclein Non-A beta component of AD amyloid Non-A4 component of amyloid precursor SNCA NACP PARK1 protein protein human Homo sapiens Human MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA DIP protein P37840 original sequence version: 124 DIP protein P37840 original sequence version: 175 DIP protein P37840 original sequence version: 178 6BB2F12128931663 snca-1 1 Alpha-synuclein 2 tag fluorescence tag visualisation by fluorescence tag fluorescence predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified fusion protein fusion protein fusion protein undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined Stoichiometry: 20.0 direct interaction direct interaction mint We first tested the ability of 13 polyphenols and black tea extract (Table 1) to antagonize the aggregation of alpha-synuclein into type-I oligomers (Fig. 2A). The degree of inhibition by the various compounds was wide-ranging, from very strong inhibition (e.g. BTE = 0.4% and Mor = 0.7%), to strong (e.g. Myr = 10%, Quer = 12%), moderate (e.g. RA = 45%, Resv = 47%), and relatively weak (e.g. Gen = 68.6%, Api = 65.1%); this feature would later prove useful in deducing structure-activity relationships. Nine compounds namely, BTE (see also Fig. 1, 8 lower panels), Mor, TA, Baic, NDGA, EGCG, Gink, Myr and Quer blocked type-I &#945;S oligomer formation to less than 20% of the control value, the latter representing aggregation in the presence of DMSO only. f1 f2a f3a The thirteen polyphenols and BTE listed in Table 1 (excluding scutellarein) were next tested for their ability to disaggregate pre-formed &#945;S oligomeric structures, the latter induced either by DMSO alone (type-I; Fig. 3A), or with the inclusion of ferric iron (type-II; Fig. 3B). It was found that Baic, EGCG, Myr, NDGA and BTE significantly disrupted both types of oligomers to <20 % of their initial aggregated state. snca-1 1 Alpha-synuclein 2 tag fluorescence tag visualisation by fluorescence tag fluorescence predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified fusion protein fusion protein fusion protein undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined Stoichiometry: 100.0 direct interaction direct interaction mint Aggregation of &#945;S occurs more strongly and results in larger type-II oligomers when ferric iron is added to the reaction mixture (Fig. 1). Thus, we selected the best ten compounds from the previous assay, and assessed their ability to antagonize &#945;S aggregation in the presence of Fe3+ ions as well. A broad range of inhibition was again observed, with six compounds blocking type-II &#945;S oligomer formation to lower than 20% of the control value (Fig. 2B): Baic (2.62 % ± 0.6), NDGA (7.96 % ± 1.1), Myr (10.12 % ± 0.7), EGCG (10.13 % ± 1), BTE (15.9 % ± 4.4), and TA (18.9 % ± 1) f1 f2b f3b f5 f6 The thirteen polyphenols and BTE listed in Table 1 (excluding scutellarein) were next tested for their ability to disaggregate pre-formed &#945;S oligomeric structures, the latter induced either by DMSO alone (type-I; Fig. 3A), or with the inclusion of ferric iron (type-II; Fig. 3B). It was found that Baic, EGCG, Myr, NDGA and BTE significantly disrupted both types of oligomers to <20 % of their initial aggregated state.