Academic
Publications
Synthesis and activity of fibrillogenesis peptide inhibitors related to the 17–21 β-amyloid sequence

Synthesis and activity of fibrillogenesis peptide inhibitors related to the 17–21 β-amyloid sequence,10.1016/j.ejmech.2008.03.036,European Journal of

Synthesis and activity of fibrillogenesis peptide inhibitors related to the 17–21 β-amyloid sequence   (Citations: 2)
BibTex | RIS | RefWorks Download
Peptide derivatives 1–5, incorporating synthetic non-proteinogenic amino acids, related to the β-amyloid 17–21 fragment of the amyloidogenic Aβ1–40, and the N-protected decapeptide 6, corresponding to a dimeric sequence of the same fragment, have been synthesized. These compounds were designed by using Soto's pentapeptide Ac–LPFFD–NH2 (iAβ5p) as lead compound. Their activity as inhibitors of fibrillogenesis and stability against enzymatic degradation have been determined. Compounds 1, 5 and 6 are potent inhibitors in comparison to the lead compound. Exposure to chymotrypsin of peptide derivatives 1–5, all containing unnatural amino acids, shows increased stability as compared with iAβ5p and 6. Conformational properties of the new compounds have been determined by CD and FT-IR spectroscopies.
Journal: European Journal of Medicinal Chemistry - EUR J MED CHEM , vol. 44, no. 1, pp. 179-189, 2009
Cumulative Annual
View Publication
The following links allow you to view full publications. These links are maintained by other sources not affiliated with Microsoft Academic Search.
Sort by: