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Effect of agitation on the peptide fibrillization: Alzheimer's amyloid‐ β peptide 1‐42 but not amylin and insulin fibrils can grow under quiescent conditions
Author(s) -
Tiiman Ann,
Noormägi Andra,
Friedemann Merlin,
Krishtal Jekaterina,
Palumaa Peep,
Tõugu Vello
Publication year - 2013
Publication title -
journal of peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 66
eISSN - 1099-1387
pISSN - 1075-2617
DOI - 10.1002/psc.2513
Subject(s) - amylin , fibril , peptide , chemistry , amyloid (mycology) , amyloid fibril , in vitro , insulin , biophysics , in vivo , biochemistry , amyloid β , medicine , endocrinology , biology , inorganic chemistry , microbiology and biotechnology , disease , islet
Many peptides and proteins can form fibrillar aggregates in vitro , but only a limited number of them are forming pathological amyloid structures in vivo . We studied the fibrillization of four peptides – Alzheimer's amyloid‐ β (A β ) 1‐40 and 1‐42, amylin and insulin. In all cases, intensive mechanical agitation of the solution initiated fast fibrillization. However, when the mixing was stopped during the fibril growth phase, the fibrillization of amylin and insulin was practically stopped, and the rate for A β 40 substantially decreased, whereas the fibrillization of A β 42 peptide continued to proceed with almost the same rate as in the agitated conditions. The reason for the different sensitivity of the in vitro fibrillization of these peptides towards agitation in the fibril growth phase remains elusive. Copyright © 2013 European Peptide Society and John Wiley & Sons, Ltd.