Abstract:
:Various structural models for amyloid β fibrils have been derived from a variety of experimental techniques. However, these models cannot differentiate between the relative position of the two arms of the β hairpin called the stagger. Amyloid fibrils of various hierarchical levels form left-handed helices composed of β sheets. However it is unclear if positive, negative and zero staggers all form the macroscopic left-handed helices. To address this issue we have conducted extensive molecular dynamics simulations of amyloid β sheets of various staggers and shown that only negative staggers lead to the experimentally observed left-handed helices while positive staggers generate the incorrect right-handed helices. This result suggests that the negative staggers are physiologically relevant structure of the amyloid β fibrils.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
GhattyVenkataKrishna PK,Uberbacher EC,Cheng Xdoi
10.1016/j.febslet.2013.06.050subject
Has Abstractpub_date
2013-08-19 00:00:00pages
2649-55issue
16eissn
0014-5793issn
1873-3468pii
S0014-5793(13)00508-5journal_volume
587pub_type
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