{"id":581,"date":"2018-10-16T13:07:39","date_gmt":"2018-10-16T13:07:39","guid":{"rendered":"https:\/\/www.mbc.manchester.ac.uk\/barrangroup\/?p=581"},"modified":"2019-07-08T09:12:26","modified_gmt":"2019-07-08T09:12:26","slug":"initial-steps-of-amyloidogenic-peptide-assembly-revealed-by-cold-ion-spectroscopy","status":"publish","type":"post","link":"https:\/\/www.mbc.manchester.ac.uk\/barrangroup\/2018\/10\/16\/initial-steps-of-amyloidogenic-peptide-assembly-revealed-by-cold-ion-spectroscopy\/","title":{"rendered":"Initial Steps of Amyloidogenic Peptide Assembly Revealed by Cold-Ion Spectroscopy"},"content":{"rendered":"

The early stages of fibril formation are difficult to capture in solution. We use cold\u2010ion spectroscopy to examine an 11\u2010residue peptide derived from the protein transthyretin and clusters of this fibre\u2010forming peptide containing up to five units in the gas phase. For each oligomer, the UV spectra exhibit distinct changes in the electronic environment of aromatic residues in this peptide compared to that of the monomer and in the bulk solution. The UV spectra of the tetra\u2010 and pentamer are superimposable but differ significantly from the spectra of the monomer and trimer. Such a spectral evolution suggests that a common structural motif is formed as early as the tetramer. The presence of this stable motif is further supported by the low conformational heterogeneity of the tetra\u2010 and pentamer, revealed from their IR spectra. From comparison of the IR\u2010spectra in the gas and condensed phases, we propose putative assignments for the dominant motif in the oligomers.<\/p>\n

\"\"<\/p>\n

Jakub Ujma,\u00a0Vladimir Kopysov,\u00a0Natalia S. Nagornova,\u00a0Lukasz G. Migas,\u00a0Maria Giovanna Lizio,\u00a0Ewan W.Blanch,\u00a0Cait MacPhee,\u00a0Oleg V. Boyarkin\u00a0and\u00a0Perdita E. Barran<\/em><\/div>\n
https:\/\/doi.org\/10.1002\/anie.201710188<\/a><\/div>\n","protected":false},"excerpt":{"rendered":"

The early stages of fibril formation are difficult to capture in solution. We use cold\u2010ion spectroscopy to examine an 11\u2010residue peptide derived from the protein transthyretin and clusters of this fibre\u2010forming peptide containing up to five units in the gas phase. For each oligomer, the UV spectra exhibit distinct changes in the electronic environment of … <\/p>\n

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