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Inhibition of Aβ42 aggregation using peptides selected from combinatorial libraries
Author(s) -
Baine Michael,
Georgie Daniel S.,
Shiferraw Elelta Z.,
Nguyen Theresa P. T.,
Nogaj Luiza A.,
Moffet David A.
Publication year - 2009
Publication title -
journal of peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 66
eISSN - 1099-1387
pISSN - 1075-2617
DOI - 10.1002/psc.1150
Subject(s) - peptide , in vivo , peptide library , chemistry , in vitro , amyloid (mycology) , biochemistry , computational biology , biology , peptide sequence , microbiology and biotechnology , gene , inorganic chemistry
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. Copyright © 2009 European Peptide Society and John Wiley & Sons, Ltd.