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 Quenched hydrogen/deuterium exchange NMR characterization of amyloid-beta peptide aggregates formed in the presence of Cu2+ or Zn2+. Quenched hydrogen/deuterium exchange NMR characterization of amyloid-beta peptide aggregates formed in the presence of Cu2+ or Zn2+. FEBS J. (1742-464X) 2009 Olofsson A., Lindhagen-Persson M., Vestling M., Sauer-Eriksson AE., Ohman A. anders.olofsson@medchem.umu.se in vitro In vitro biophysical biophysical peptide synthesis peptide synthesis Olofsson A., Lindhagen-Persson M., Vestling M., Sauer-Eriksson AE., Ohman A. anders.olofsson@medchem.umu.se FEBS J. (1742-464X) 2009 Quenched hydrogen/deuterium exchange NMR characterization of amyloid-beta peptide aggregates formed in the presence of Cu2+ or Zn2+. Quenched hydrogen/deuterium exchange NMR characterization of amyloid-beta peptide aggregates formed in the presence of Cu2+ or Zn2+. FEBS J. (1742-464X) 2009 Olofsson A., Lindhagen-Persson M., Vestling M., Sauer-Eriksson AE., Ohman A. anders.olofsson@medchem.umu.se in vitro In vitro atomic force microsc atomic force microscopy AFM AFM atomic force microsc peptide synthesis peptide synthesis Olofsson A., Lindhagen-Persson M., Vestling M., Sauer-Eriksson AE., Ohman A. anders.olofsson@medchem.umu.se FEBS J. (1742-464X) 2009 Quenched hydrogen/deuterium exchange NMR characterization of amyloid-beta peptide aggregates formed in the presence of Cu2+ or Zn2+. Quenched hydrogen/deuterium exchange NMR characterization of amyloid-beta peptide aggregates formed in the presence of Cu2+ or Zn2+. FEBS J. (1742-464X) 2009 Olofsson A., Lindhagen-Persson M., Vestling M., Sauer-Eriksson AE., Ohman A. anders.olofsson@medchem.umu.se in vitro In vitro nmr nuclear magnetic resonance NMR NMR nmr peptide synthesis peptide synthesis Olofsson A., Lindhagen-Persson M., Vestling M., Sauer-Eriksson AE., Ohman A. anders.olofsson@medchem.umu.se FEBS J. (1742-464X) 2009 Quenched hydrogen/deuterium exchange NMR characterization of amyloid-beta peptide aggregates formed in the presence of Cu2+ or Zn2+. Quenched hydrogen/deuterium exchange NMR characterization of amyloid-beta peptide aggregates formed in the presence of Cu2+ or Zn2+. FEBS J. (1742-464X) 2009 Olofsson A., Lindhagen-Persson M., Vestling M., Sauer-Eriksson AE., Ohman A. anders.olofsson@medchem.umu.se in vitro In vitro fluorescence fluorescence technology fluorescence peptide synthesis peptide synthesis Olofsson A., Lindhagen-Persson M., Vestling M., Sauer-Eriksson AE., Ohman A. anders.olofsson@medchem.umu.se FEBS J. (1742-464X) 2009 Quenched hydrogen/deuterium exchange NMR characterization of amyloid-beta peptide aggregates formed in the presence of Cu2+ or Zn2+. Quenched hydrogen/deuterium exchange NMR characterization of amyloid-beta peptide aggregates formed in the presence of Cu2+ or Zn2+. FEBS J. (1742-464X) 2009 Olofsson A., Lindhagen-Persson M., Vestling M., Sauer-Eriksson AE., Ohman A. anders.olofsson@medchem.umu.se in vitro In vitro cd circular dichroism CD CD cd peptide synthesis peptide synthesis Olofsson A., Lindhagen-Persson M., Vestling M., Sauer-Eriksson AE., Ohman A. anders.olofsson@medchem.umu.se FEBS J. (1742-464X) 2009 a4_human Amyloid-beta precursor protein APP A4 AD1 Alzheimer disease amyloid protein ABPP PreA4 Cerebral vascular amyloid peptide Protease nexin-II APPI Amyloid precursor protein Amyloid-beta A4 protein Alzheimer disease amyloid A4 protein homolog Amyloid-beta (A4) precursor protein protein protein human Homo sapiens Human MLPGLALLLLAAWTARALEVPTDGNAGLLAEPQIAMFCGRLNMHMNVQNGKWDSDPSGTKTCIDTKEGILQYCQEVYPELQITNVVEANQPVTIQNWCKRGRKQCKTHPHFVIPYRCLVGEFVSDALLVPDKCKFLHQERMDVCETHLHWHTVAKETCSEKSTNLHDYGMLLPCGIDKFRGVEFVCCPLAEESDNVDSADAEEDDSDVWWGGADTDYADGSEDKVVEVAEEEEVAEVEEEEADDDEDDEDGDEVEEEAEEPYEEATERTTSIATTTTTTTESVEEVVREVCSEQAETGPCRAMISRWYFDVTEGKCAPFFYGGCGGNRNNFDTEEYCMAVCGSAMSQSLLKTTQEPLARDPVKLPTTAASTPDAVDKYLETPGDENEHAHFQKAKERLEAKHRERMSQVMREWEEAERQAKNLPKADKKAVIQHFQEKVESLEQEAANERQQLVETHMARVEAMLNDRRRLALENYITALQAVPPRPRHVFNMLKKYVRAEQKDRQHTLKHFEHVRMVDPKKAAQIRSQVMTHLRVIYERMNQSLSLLYNVPAVAEEIQDEVDELLQKEQNYSDDVLANMISEPRISYGNDALMPSLTETKTTVELLPVNGEFSLDDLQPWHSFGADSVPANTENEVEPVDARPAADRGLTTRPGSGLTNIKTEEISEVKMDAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIATVIVITLVMLKKKQYTSIHHGVVEVDAAVTPEERHLSKMQQNGYENPTYKFFEQMQN DIP protein P05067 original sequence version: 160 DIP protein P05067 original sequence version: 207 DIP protein P05067 original sequence version: 185 DIP protein P05067 original sequence version: 188 A12EE761403740F5 app-1 5 Abeta 6 peptide synthesis peptide synthesis predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain direct interaction direct interaction F1C mint Aβ(1-42) forms aggregates in the presence of Cu2+ or Zn2+ or fibrils in the presence of EDTA. app-1 5 Abeta 6 peptide synthesis peptide synthesis predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain direct interaction direct interaction F1C mint Aβ(1-40 ) forms aggregates in the presence of Cu2+ or Zn2+ or fibrils in the presence of EDTA. app-1 1 Abeta 6 peptide synthesis peptide synthesis predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain direct interaction direct interaction F1A mint Turbidity measurements show that the aggregation rates of both Aβ(1-40) and Aβ(1-42) are significantly increased in the presence of either Cu2+ or Zn2+ (Figure 1a). app-1 1 Abeta 6 peptide synthesis peptide synthesis predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain direct interaction direct interaction F1A mint Turbidity measurements show that the aggregation rates of both Aβ(1-40) and Aβ(1-42) are significantly increased in the presence of either Cu2+ or Zn2+ (Figure 1a). app-1 3 Abeta 6 peptide synthesis peptide synthesis predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain direct interaction direct interaction F3 mint Samples verified by AFM and ThT analysis to contain the fibrillar forms of Aβ(1-40) and Aβ(1-42) (fibrils formed in presence of EDTA) displayed amide protection patterns with two bell-shaped protected regions (Figures 3c and f). Aβ(1-40) fibrils showed partial to full protection for residues Glu3-Ser26 and Gly29-Val40, separated by exposed residues in the turn region centered at Asn27-Lys28 (Figure 3c), whereas the protection pattern of the fibrillar form of Aβ(1-42) included residues Phe4-Arg5, Tyr10-Ser26 and Gly29-Ala42(Figure 3f). The degree of protection in the N-terminal region of Aβ(1-42) is notably lower than in Aβ(1-40)... The presence of either Cu2+ or Zn2+ during aggregate/fibril growth has a significant impact on the solvent protection pattern for both Aβ(1-40) and Aβ(1-42). When compared to the protection ratios in the absence of metal (Figures 3c and f), the overall protection ratio in the presence of metal is significantly reduced (Figures 3a,b,d and e). app-1 3 Abeta 6 peptide synthesis peptide synthesis predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain direct interaction direct interaction F3 mint Samples verified by AFM and ThT analysis to contain the fibrillar forms of Aβ(1-40) and Aβ(1-42) (fibrils formed in presence of EDTA) displayed amide protection patterns with two bell-shaped protected regions (Figures 3c and f). Aβ(1-40) fibrils showed partial to full protection for residues Glu3-Ser26 and Gly29-Val40, separated by exposed residues in the turn region centered at Asn27-Lys28 (Figure 3c), whereas the protection pattern of the fibrillar form of Aβ(1-42) included residues Phe4-Arg5, Tyr10-Ser26 and Gly29-Ala42(Figure 3f). The degree of protection in the N-terminal region of Aβ(1-42) is notably lower than in Aβ(1-40)... The presence of either Cu2+ or Zn2+ during aggregate/fibril growth has a significant impact on the solvent protection pattern for both Aβ(1-40) and Aβ(1-42). When compared to the protection ratios in the absence of metal (Figures 3c and f), the overall protection ratio in the presence of metal is significantly reduced (Figures 3a,b,d and e). app-1 4 Abeta 6 peptide synthesis peptide synthesis predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain direct interaction direct interaction F1B mint The amount of amyloid or amyloid-like structure within the different Aβ-assemblies was quantified by ThT fluorescence. With Cu2+ present approximately 10% of the normal fibrillar ThT signal for both Aβ(1-40) and Aβ(1-42) aggregates was detected, while zinc-induced aggregates resulted in a larger ThT-response corresponding to approximately 40% of the fibrillar counterpart (Figure 1b). app-1 4 Abeta 6 peptide synthesis peptide synthesis predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain direct interaction direct interaction F1B mint The amount of amyloid or amyloid-like structure within the different Aβ-assemblies was quantified by ThT fluorescence. With Cu2+ present approximately 10% of the normal fibrillar ThT signal for both Aβ(1-40) and Aβ(1-42) aggregates was detected, while zinc-induced aggregates resulted in a larger ThT-response corresponding to approximately 40% of the fibrillar counterpart (Figure 1b). app-1 2 Abeta 6 peptide synthesis peptide synthesis predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain direct interaction direct interaction F2 mint The aggregates of Aβ(1-40) and Aβ(1-42) formed in the presence of a chelating agent gave rise to the classical fibrillar morphology with an average fibril diameter of around 7 nm. For both Aβ(1-40) and Aβ(1-42) the presence of divalent metal ions efficiently inhibited fibril formation and, as expected, resulted in more amorphous assemblies. app-1 2 Abeta 6 peptide synthesis peptide synthesis predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain direct interaction direct interaction F2 mint The aggregates of Aβ(1-40) and Aβ(1-42) formed in the presence of a chelating agent gave rise to the classical fibrillar morphology with an average fibril diameter of around 7 nm. For both Aβ(1-40) and Aβ(1-42) the presence of divalent metal ions efficiently inhibited fibril formation and, as expected, resulted in more amorphous assemblies.