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 Peptides that form β-sheets on hydrophobic surfaces accelerate surface-induced insulin amyloidal aggregation. Peptides that form β-sheets on hydrophobic surfaces accelerate surface-induced insulin amyloidal aggregation. FEBS Lett. (0014-5793) 2013 imex curation Nault L., Vendrely C., Bréchet Y., Bruckert F., Weidenhaupt M. Only protein-protein interactions in vitro In vitro fluorescence fluorescence technology fluorescence predetermined predetermined participant predetermined Nault L., Vendrely C., Bréchet Y., Bruckert F., Weidenhaupt M. Accepted 2013-AUG-29 by MARTA FEBS Lett. (0014-5793) 2013 Only protein-protein interactions imex curation ins_human Insulin INS protein protein human Homo sapiens Human MALWMRLLPLLALLALWGPDPAAAFVNQHLCGSHLVEALYLVCGERGFFYTPKTRREAEDLQVGQVELGGGPGAGSLQPLALEGSLQKRGIVEQCCTSICSLYQLENYCN DIP protein P01308 original sequence version: 184 DIP protein P01308 original sequence version: 104 DIP protein P01308 original sequence version: 177 Insulin decreases blood glucose concentration. It increases cell permeability to monosaccharides, amino acids and fatty acids. It accelerates glycolysis, the pentose phosphate cycle, and glycogen synthesis in liver mint homomint Defects in INS are the cause of familial hyperproinsulinemia [MIM:176730] C2C3B23B85E520E5 ins-ins-19 1 HI 2 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified HI 2 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified direct interaction direct interaction t1 homomint mint The strong effect of the LVEALYL peptide on HI aggregation kinetics prompted us to study different peptide variants (Table 1). All experiments were done at the same peptide (8.6 μM) and HI (86 μM) concentrations. None of the peptides studied here aggregates on its own, nor triggers HI aggregation in the presence of PEG-coated surfaces, confirming that the kinetic enhancement is dependent on the presence of hydrophobic surfaces. Among the peptides studied, the swapped peptide LVAELYL, where the third and fourth amino acid are exchanged, exhibits a remarkably short lag time (0.4 h). This peptide binds also strongly to hydrophobic surfaces (0.1 μg) and pre-adsorption reduces the lag time of HI aggregation down to 2.3 h (Table 1).