Comparisons of the NACP self-oligomerizations induced by Aβ25-35 in the presence of dicyclohexylcarbodiimide and N-(ethoxycarbonyl)-2-ethoxy 1, 2-dihydroquinoline

摘要: NACP, the precursor protein of non-amyloid β/A4 (Aβ) component Alzheimer's disease (AD) amyloid, also known as α-synuclein was shown to undergo self-oligomerization only in presence a modified Aβ fragment (residues 25–35) by using relatively hydrophobic coupling reagent, dicyclohexylcarbodiimide (DCCD). Since oligomerization not required high concentration DCCD but its efficiency suppressed even at slightly basic pH 7.5, another reagent called N-(ethoxycarbonyl)-2-ethoxy-1,2-dihydroquinoline (EEDQ) examined order make use this technique access functional aspects NACP vitro exploring more accurate and reproducible reaction conditions. The EEDQ gave rise Aβ25-35 among variously peptides. about three times effective than terms optimal visualize oligomers. In addition, oligomerizing potency affected condition. Although physiological pathological significance are currently unknown, dramatic phenomenon visualization could shed light on determination molecular relationships with various intracellular or extracellular biomolecules related conditions Parkinson's diseases.