Abstract Sixty picomoles of human serum albumin (HSA) was immobilized on a glycidylmethacrylate (GMA) capillary column previously developed by our group to study its binding with two universal cancer peptides (UCPs). Zonal HPLC experiments demonstrated that UCP2 and UCP4 have 1:1 interaction at the well-known site I of HSA with similar affinities in the micromolar range. At pH 7.4 UCP2 and UCP4 bound to HSA site I with negative ΔH values increasing with increasing temperature leading to positive heat capacity changes (UCP2: ΔC p=1.06 kJ/mol/K; UCP4: ΔC p=0.53 kJ/mol/K). The sign and magnitude of these thermodynamic data were explained by the burial of the polar groups of the peptide inside the hydrophobic binding pocket of HSA leading to coil helix transition upon the binding. The strong linear coefficient (r 2 = 0.995) for the plot comparing the immunogenicity index (II) between a series of four UCPs against the enthalpy gain confirmed a high degree of similarity for the mechanism of immunogenicity of these short peptides. The positive slope (+2.59) indicated that at physiological pH (7.4), the helix gain upon UCPs/HSA binding promoted the immunogenicity of the peptide vaccine. Graphical Abstract

中文翻译：

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用人血清白蛋白功能化的有机整体毛细管柱及其在纳米色谱研究中与通用癌肽结合及其对免疫原性影响的应用

摘要 将 60 皮摩尔人血清白蛋白 (HSA) 固定在我们小组先前开发的甲基丙烯酸缩水甘油酯 (GMA) 毛细管柱上，以研究其与两种通用癌症肽 (UCP) 的结合。带状 HPLC 实验表明 UCP2 和 UCP4 在 HSA 的众所周知的位点 I 处具有 1:1 的相互作用，在微摩尔范围内具有相似的亲和力。在 pH 7.4 时，UCP2 和 UCP4 与 HSA 位点 I 结合，负 ΔH 值随温度升高而增加，导致正热容变化（UCP2：ΔC p=1.06 kJ/mol/K；UCP4：ΔC p=0.53 kJ/mol/K） . 这些热力学数据的符号和大小可以通过将肽的极性基团掩埋在 HSA 的疏水性结合口袋内来解释，导致结合时卷曲螺旋转变。强线性系数（r 2 = 0。995) 的图比较了一系列四种 UCP 之间的免疫原性指数 (II) 与焓增益，证实了这些短肽的免疫原性机制的高度相似性。正斜率 (+2.59) 表明在生理 pH 值 (7.4) 下，UCP/HSA 结合后的螺旋增益促进了肽疫苗的免疫原性。图形概要