905438-75-7Relevant academic research and scientific papers
β-sheet breaker peptides containing α,β- dehydrophenylalanine: Synthesis and in vitro activity studies
Giordano, Cesare,Punzi, Pasqualina,Lori, Clorinda,Chiaraluce, Roberta,Consalvi, Valerio
, p. 1036 - 1043 (2014)
The synthesis and fibrillogenesis-inhibiting activity of the new peptide derivatives 1-6, containing α,β-unsaturated phenylalanines, are reported. These compounds are related to the pentapeptide Ac-LPFFD-NH 2 (iAβ5p), which was designed by Soto and co-workers and is commonly accepted as a lead compound for fibrillogenesis inhibition. Their activities are determined by Thioflavin T binding assay, far-UV circular dichroism (CD) spectroscopy, and SEM; in addition, their structures in solution are studied through far-UV CD and FTIR spectroscopy. The presence of two α,β-unsaturated phenylalanines increases the fibrillogenesis inhibiting activity significantly in comparison with the lead compound. The interactions between the Aβ1-40 and the inhibitors using electrospray ionization mass spectrometry are also studied. The analyses prove the presence of noncovalent complexes of Aβ1-40 with iAβ5p and its derivatives 1-3 with stoichiometries of 1:1 and 2:1, and the results are independent of time and Aβ1-40/inhibitor ratio.
