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Effect of the Surface Chemistry of Insulin Fibrils on the Aggregation Rate
Author(s) -
Hsieh Shuchen,
Hsieh ChiungWen,
Chou HsuanHung,
Chang ChiungWen,
Chu LingYa
Publication year - 2014
Publication title -
chemphyschem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.016
H-Index - 140
eISSN - 1439-7641
pISSN - 1439-4235
DOI - 10.1002/cphc.201300838
Subject(s) - fibril , chemistry , atomic force microscopy , amyloid fibril , biophysics , crystallography , chemical engineering , nanotechnology , biochemistry , amyloid β , materials science , medicine , disease , pathology , biology , engineering
Structure transition cascade: Insulin fibrils undergo a secondary structural transition—from the α‐rich to the β‐rich form—upon progressively increasing the incubation time from 0.5 to ten hours. Atomic force microscopy measurements show that the fibril surface chemistry changes from hydrophilic to hydrophobic and the aggregation rate increases fivefold.