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Article
Inhibition of Aβ42 aggregation using peptides selected from combinatorial libraries
Journal of Peptide Science
  • Michael Baine, Loyola Marymount University
  • Daniel S. Georgie, Loyola Marymount University
  • Elelta Z. Shiferraw, Loyola Marymount University
  • Theresa P. T. Nguyen, Loyola Marymount University
  • Luiza A. Nogaj, Loyola Marymount University
  • David A. Moffet, Loyola Marymount University
Document Type
Article - pre-print
Publication Date
6-1-2009
Disciplines
Abstract

Increasing evidence suggests that the aggregation of the small peptide Aβ42 plays an important role in the development of Alzheimer’s disease. Inhibiting the initial aggregation of Aβ42 may be an effective treatment for preventing, or slowing, the onset of the disease. Using an in vivo screen based on the enzyme EGFP, we have searched through two combinatorially diverse peptide libraries to identify peptides capable of inhibiting Aβ42 aggregation. From this initial screen, three candidate peptides were selected and characterized. ThT studies indicated that the selected peptides were capable of inhibiting amyloid aggregation. Additional ThT studies showed that one of the selected peptides was capable of disaggregating preformed Aβ42 fibers.

Publisher Statement

This is an author-manuscript of an article accepted for publication in Journal of Peptide Science following peer review. The published version of this record is available online at doi: doi:10.1002/psc.1150.

Citation Information
Baine M, Georgie DS, Shiferraw EZ, Nguyen TPT, Nogaj LA, Moffet DA. Inhibition of Aβ42 aggregation using peptides selected from combinatorial libraries. Journal of peptide science : an official publication of the European Peptide Society. 2009;15(8):499-503. doi:10.1002/psc.1150.