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Visible‐Light Microscopic Discovery of Up to 150 μm Long Helical Amyloid Fibrils Built of the Dodecapeptide H‐(Val‐Ala‐Leu) 4 ‐OH and of Decapeptides Derived from Insulin
Author(s) -
Świontek Monika,
Kamiński Zbigniew J.,
Kolesińska Beata,
Seebach Dieter
Publication year - 2016
Publication title -
chemistry and biodiversity
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.427
H-Index - 70
eISSN - 1612-1880
pISSN - 1612-1872
DOI - 10.1002/cbdv.201600167
Subject(s) - chemistry , fibril , peptide , amyloid (mycology) , amyloid fibril , biophysics , helicity , crystallography , biochemistry , amyloid β , medicine , physics , biology , inorganic chemistry , disease , particle physics
In the formation of amyloid fibrils from small peptides, the appearance of superhelices of ( P )‐ or ( M )‐helicity has been observed for the first time; high concentrations of the peptides and extended periods of incubation at physiological pH appear to be important for this phenomenon. In view of the general importance of peptide and protein aggregation, we give a brief overview with selected examples for demonstration.