Atomic force microscopy study of human amylin (20-29) fibrils.
Here we present atomic force microscopy images of the fibrils formed by human amylin(20-29). This peptide is a fragment of the polypeptide amylin, the major proteinaceous component of amyloid deposits found in cases of type-II diabetes mellitus. Our results demonstrate that the amylin(20-29) peptide fragment forms amyloid-like fibrils that display polymorphic structures. Twisting along the axis of fibrils was often observed in fibrils aged for 6 hours but disappeared in mature fibrils aged for longer time periods.
Sedman
Victoria L
VL
Laboratory of Biophysics and Surface Analysis, School of Pharmacy, The University of Nottingham, Nottingham. NG7 2RD UK.
Allen
Stephanie
S
Chan
Weng C
WC
Davies
Martyn C
MC
Roberts
Clive J
CJ
Tendler
Saul J B
SJ
Williams
Philip M
PM
D000595:Amino Acid Sequence; D000682:Amyloid / Q000737:chemistry / Q000648:ultrastructure*; D006801:Humans; D018625:Microscopy, Atomic Force; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry / Q000648:ultrastructure*; D013997:Time Factors
D000682:Amyloid; D010446:Peptide Fragments; C117453:amylin (20-29)