数据日期 2026-10-29 · 生成时间 2026-10-29 06:03
研究问题
Aβ peptides can aggregate into soluble oligomers, protofibrils, and mature amyloid fibrils, although the relative contributions of different Aβ assemblies to disease progression remain incompletely understood [18].
方法
Working solutions were prepared by diluting stocks into 20 mM HEPES/KOH buffer, pH 7.4, to obtain final ligand concentrations of 0–1.0 µM.；Fluorescence titrations were performed in 20 mM HEPES/KOH buffer, pH 7.4 containing 0.1 µM Aβ1-42 protein concentration.；The interaction of Aβ1-42- α-halogenated curcumins were measured by direct protein fluorescence.；Samples were excited at 280 nm, and emission was measured from 300 to 400 nm using excitation and emission slit widths of 5 and 10 nm, respectively.
核心结论
At the highest ratios examined, fluorescence quenching reached 55% for curcumin, 72% for α-bromocurcumin, and 90% for α-chlorocurcumin.；Relative to the untreated control (100.00 ± 8.00%), the signal decreased to 94.16 ± 6.60%, 90.00 ± 4.00%, 85.80 ± 5.80%, and 83.00 ± 3.70% at curcumin concentrations of 100, 200, 500, and 1000 nM, respectively (mean ± SE).；These values correspond to reductions of 5.84%, 10.00%, 14.20%, and 17.00%, supporting a concentration-dependent attenuation of the β-sheet-associated CD signal. ‖ 结论：Overall, the findings support differential binding and measurable conformational changes in Aβ1-42 associated with the α-halogenated curcumins.
局限
全文未设独立 limitations 节；结构上为非 RCT 设计，因果推断强度受限。
对本项目的价值
★★☆☆☆ 脑老化是最大未满足需求，也是终点最难量化的领域；biomarker 与认知读数选择最敏感。
全文来源
PMC JATS 全文（正文 47,061 字符，已过标题/DOI 逐字归属校验）
原文题录
- 英文标题：α-Halogenated Curcumins Enhance the Binding Affinity and Induced Structural Alterations to Amyloid-β Protein in Alzheimer's Disease.
- 期刊与标识：Int J Mol Sci · PMID 42942122 · DOI 10.3390/ijms27209355**
A 级证据分级：A 级（同行评议人体研究）
本文属人体研究证据，但需注意：观察性或小样本干预的结论不等于已证实临床获益；效应量与长期安全性仍需更大规模、更长随访的试验验证。
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