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University of California, Irvine
It is quite likely that amino-terminal deletions could also have an impact on the aggregation of Aβ. Christian Pike and Carl Cotman showed that amino-terminally truncated peptides aggregate faster than the corresponding full-length peptides. In addition, conformational transitions in the amino terminus seem to play a role in fibril formation, because Beka Solomon has shown that antibodies directed against the amino terminus cause the disaggregation of fibrils. However, it is not clear that amino-terminally truncated species are the sole or primary pathogenic species, as amino-terminal antibodies seem to be effective in reducing AD type pathology in Tg mice.
References:
Pike CJ, Overman MJ, Cotman CW. Amino-terminal deletions enhance aggregation of beta-amyloid peptides in vitro. J Biol Chem. 1995 Oct 13;270(41):23895-8. PubMed.
Solomon B, Koppel R, Frankel D, Hanan-Aharon E. Disaggregation of Alzheimer beta-amyloid by site-directed mAb. Proc Natl Acad Sci U S A. 1997 Apr 15;94(8):4109-12. PubMed.
Frenkel D, Balass M, Katchalski-Katzir E, Solomon B. High affinity binding of monoclonal antibodies to the sequential epitope EFRH of beta-amyloid peptide is essential for modulation of fibrillar aggregation. J Neuroimmunol. 1999 Mar 1;95(1-2):136-42. PubMed.
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