This study aimed to explore the effect of secondary lipid oxidation products (SLOPs) on Hemoglobin (Hb) in chicken model. The fluorescence quenching technique and molecular docking were employed, and the apparent binding constants K_sv and the binding site numbers of SLOPs with Hb were calculated. The results revealed that three SLOPs (hexanal, benzaldehyde, and 2-pentanone) obviously promoted the oxidation of Hb, which is consistent with the change of Hb hydrophobicity, particle size, PdI and zeta potential. The SLOPs strongly quenched the intrinsic fluorescence of Hb and triggered the alterations in the Hb structure. Hydrophobic interaction was the main force between SLOPs and Hb. Among the three SLOPs, hexanal demonstrated more stronger oxidation on Hb, which is closely related to its hydrophobic ability and structure characteristic, especially 10 μM hexanal is more prone to form an obvious unfolded structure and caused molecular aggregation than lower concentrations.

本研究旨在探讨次级脂质氧化产物（SLOPs）对鸡模型血红蛋白（Hb）的影响。采用荧光猝灭技术和分子对接，表观结合常数K _sv并计算 SLOPs 与 Hb 的结合位点数。结果表明，三种SLOPs（己醛、苯甲醛和2-戊酮）明显促进了Hb的氧化，这与Hb疏水性、粒径、PdI和zeta电位的变化是一致的。SLOPs 强烈淬灭 Hb 的固有荧光并引发 Hb 结构的改变。疏水相互作用是SLOPs和Hb之间的主要力量。在三种SLOPs中，己醛对Hb的氧化作用更强，这与其疏水能力和结构特征密切相关，尤其是10 μM的己醛比低浓度更容易形成明显的未折叠结构并引起分子聚集。