کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
1398040 | 1501205 | 2009 | 11 صفحه PDF | دانلود رایگان |
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.
Synthesis, properties and activity of novel analogues (1–6) of the known Ac–Leu-Pro-Phe-Phe-Asp(OH)–NH2 (iAβ5p) fibrillogenesis pentapeptide inhibitor are reported.Figure optionsDownload as PowerPoint slide
Journal: European Journal of Medicinal Chemistry - Volume 44, Issue 1, January 2009, Pages 179–189