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 An orphan dermaseptin from frog skin reversibly assembles to amyloid-like aggregates in a pH-dependent fashion. An orphan dermaseptin from frog skin reversibly assembles to amyloid-like aggregates in a pH-dependent fashion. FEBS J. (1742-464X) 2009 imex curation Gössler-Schöfberger R., Hesser G., Muik M., Wechselberger C., Jilek A. Only protein-protein interactions in vitro In vitro biophysical biophysical predetermined predetermined participant predetermined Gössler-Schöfberger R., Hesser G., Muik M., Wechselberger C., Jilek A. FEBS J. (1742-464X) 2009 Only protein-protein interactions imex curation An orphan dermaseptin from frog skin reversibly assembles to amyloid-like aggregates in a pH-dependent fashion. An orphan dermaseptin from frog skin reversibly assembles to amyloid-like aggregates in a pH-dependent fashion. FEBS J. (1742-464X) 2009 imex curation Gössler-Schöfberger R., Hesser G., Muik M., Wechselberger C., Jilek A. Only protein-protein interactions in vitro In vitro fluorescence imaging fluorescence microscopy fluorescence imaging predetermined predetermined participant predetermined Gössler-Schöfberger R., Hesser G., Muik M., Wechselberger C., Jilek A. FEBS J. (1742-464X) 2009 Only protein-protein interactions imex curation An orphan dermaseptin from frog skin reversibly assembles to amyloid-like aggregates in a pH-dependent fashion. An orphan dermaseptin from frog skin reversibly assembles to amyloid-like aggregates in a pH-dependent fashion. FEBS J. (1742-464X) 2009 imex curation Gössler-Schöfberger R., Hesser G., Muik M., Wechselberger C., Jilek A. Only protein-protein interactions in vitro In vitro fluorescence fluorescence technology fluorescence predetermined predetermined participant predetermined Gössler-Schöfberger R., Hesser G., Muik M., Wechselberger C., Jilek A. FEBS J. (1742-464X) 2009 Only protein-protein interactions imex curation An orphan dermaseptin from frog skin reversibly assembles to amyloid-like aggregates in a pH-dependent fashion. An orphan dermaseptin from frog skin reversibly assembles to amyloid-like aggregates in a pH-dependent fashion. FEBS J. (1742-464X) 2009 imex curation Gössler-Schöfberger R., Hesser G., Muik M., Wechselberger C., Jilek A. Only protein-protein interactions in vitro In vitro cd circular dichroism CD CD cd predetermined predetermined participant predetermined Gössler-Schöfberger R., Hesser G., Muik M., Wechselberger C., Jilek A. FEBS J. (1742-464X) 2009 Only protein-protein interactions imex curation An orphan dermaseptin from frog skin reversibly assembles to amyloid-like aggregates in a pH-dependent fashion. An orphan dermaseptin from frog skin reversibly assembles to amyloid-like aggregates in a pH-dependent fashion. FEBS J. (1742-464X) 2009 imex curation Gössler-Schöfberger R., Hesser G., Muik M., Wechselberger C., Jilek A. Only protein-protein interactions in vitro In vitro electron microscopy electron microscopy Electron crystallography Electron cryomicroscopy Electron crystallography Electron cryomicroscopy predetermined predetermined participant predetermined Gössler-Schöfberger R., Hesser G., Muik M., Wechselberger C., Jilek A. FEBS J. (1742-464X) 2009 Only protein-protein interactions imex curation dru_agadc Dermaseptin PD-3-7 protein protein pacda Pachymedusa dacnicolor MSFMKKSLLLVLFLGVVSLSNCEEEKGENENEDHEEHHEEKRLLGDLLGQTSKLVNDLTDTVGSIV mint 1783028D8750C051 dms5 1 Dermaseptin 6 peptide synthesis peptide synthesis predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified direct interaction direct interaction mint f2c f4d Second, a high content of β-sheet secondary structure was detected by FTIR spectroscopy. Investigation of the second derivative of the amide I region demonstrated that maxima at 1619 and 1635 cm-1 were the most likely bands. These bands can be attributed to β-sheet structures. ...In the FTIR spectra recorded 5 minutes after the pH-shift to 6.0, a minor peak contribution (approx. 10 %) of a band at 1621 cm-1 was clearly detectable (Fig. 4). This result suggested that a significant degree of interchain hydrogen bonds is still present in the aggregates. dms5-1 2 Dermaseptin 6 peptide synthesis peptide synthesis predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified direct interaction direct interaction f2b mint aDrs aggregates after prolonged incubation at acidic pH. dms5-1 5 Dermaseptin 6 peptide synthesis peptide synthesis predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified direct interaction direct interaction f2d mint Negative stain electron-micrographs of aDrs fibrils formed at acidic pH. dms5-1 3 Dermaseptin 6 peptide synthesis peptide synthesis predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified direct interaction direct interaction mint ...aDrs aggregates after prolonged incubation at acidic pH. ...We exposed aDrs fibrils to various pH values in order to investigate their pH dependent stability. The resulting profile revealed a sharp transition point at pH 5 and a sigmoidal decrease of ThT fluorescence in the transition interval towards higher pH values (Fig. 3). f3 f4b dms5-1 4 Dermaseptin 6 peptide synthesis peptide synthesis predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified direct interaction direct interaction f4c mint CD spectra of fibrils (dashed line), aggregates formed from fibrils at pH 6.0 after 5 minutes (solid line) and soluble aDrs (dotted line).