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Enhanced aggregation and β structure of amyloid β peptide after coincubation with C1Q
Author(s) -
Webster S.,
O'Barr S.,
Rogers J.
Publication year - 1994
Publication title -
journal of neuroscience research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.72
H-Index - 160
eISSN - 1097-4547
pISSN - 0360-4012
DOI - 10.1002/jnr.490390412
Subject(s) - peptide , in vitro , in vivo , neurotoxicity , chemistry , amyloid (mycology) , biophysics , colocalization , thioflavin , complement system , protein aggregation , biochemistry , microbiology and biotechnology , biology , immunology , toxicity , alzheimer's disease , medicine , antibody , inorganic chemistry , disease , organic chemistry
Several lines of evidence now suggest that aggregation of soluble amyloid β peptide (Aβ) into a cross β sheet configuration may be an important factor in mediating potential neurotoxicity of Aβ. Synthetic Aβ has been shown to self aggregate in vitro. Here, we demonstrate that coincubation of freshly solubilized Aβ with C1q, a complement component known to bind Aβ in vitro and to colocalize with Aβ in vivo, results in as much as a 7‐fold enhancement of Aβ aggregation, as well as a 2–4‐fold enhancement of β structure within aggregates. The addition of C1q to preformed Aβ aggregates also results in significantly increased resistance to aggregate resolubilization. © 1994 Wiley‐Liss, Inc.