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首页> 外文期刊>Biophysical Chemistry: An International Journal Devoted to the Physical Chemistry of Biological Phenomena >Complexation between Cu(II) and curcumin in the presence of two different segments of amyloid beta
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Complexation between Cu(II) and curcumin in the presence of two different segments of amyloid beta

机译：Cu（II）与姜黄素在两种不同淀粉样蛋白β的不同区段之间的络合

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摘要

The natural product curcumin has been shown to play a role in preventing A(i amyloid fibril formation. This role could include chelation of transition metal ions such as Cu~(2+), known to accelerate amyloid aggregation, and/or curcumin-binding directly to the Abeta protein. To investigate these different roles, curcumin complexation to Cu~(2+) was investigated in the presence and absence of two different segments of the Abeta protein including the copper-binding (A36-14) and curcumin-binding (A(314-23) domains. Absorbance and fluorescence spectrosco-py in 90% water/10% methanol solutions showed that curcumin can bind Cu~(2+) to some extent in the presence of both segments despite strong peptide-ion interactions. Estimated Cu~(2+)-curcumin binding affinities in the absence (1.6 x 10~5 M~(-1)) and presence (7.9 x 10~4 M~(-1)) of the peptide provide quantitative support for this Cu~(2+) chelation role. With the Abeta14-23 segment, the curcumin simultaneously binds to Cu~(2+) and the peptide, demonstrating that it can play multiple roles in the prevention of amyloid formation. The stabilities of ternary peptide-Cu~(2+)-curcumin complexes were evaluated using ESI mass spectrometry and support the conclusion that curcumin can act as a weak metal ion chelator and also bind directly to the Abeta14-23 peptide segment.
机译：已显示天然产物姜黄素在预防A（I淀粉样蛋白原纤维形成中的作用。该作用可包括过渡金属离子如Cu〜（2+）的螯合，已知加速淀粉样蛋白聚集和/或姜黄素结合直接到abeta蛋白质。为了研究这些不同的作用，在存在和不存在包括铜结合（A36-14）和姜黄素结合的情况下，研究了对Cu〜（2+）的姜黄素络合。 （A（314-23）结构域。90％水/ 10％甲醇溶液中的吸光度和荧光谱分泌溶液显示，尽管存在强肽离子相互作用，姜黄素可以在某种程度上在某种程度上结合Cu〜（2+） 。估计Cu〜（2 +） - 抗蛋白结合亲和力（1.6×10〜5 m〜（-1））和存在（7.9×10〜4m〜（-1））的肽提供定量支持该Cu〜（2+）螯合作用。随着ABETA14-23段，姜黄素同时结合Cu〜（2+）和Pepti DE，证明它可以在预防淀粉样蛋白形成中发挥多种作用。使用ESI质谱法评估三元肽-Cu〜（2 +） - 姜黄素复合物的稳定性，并支持姜黄素可以用作弱金属离子螯合剂并直接与ABETA14-23肽区段结合的结论。

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