CAJ | 학술논문

在生理酸度（pH 7．4）条件下，应用荧光光谱法、紫外-可见吸收光谱法和圆二色谱法（CD）研究了赤藓红与人血清白蛋白（HSA）的相互作用及其对 HSA 结构的影响。荧光滴定实验结果表明，静态猝灭是导致 HSA 内源荧光猝灭的主要原因；位点竞争实验显示，赤藓红主要结合在 HSA 的亚结构域 IIA（site I）；计算出的热力学参数焓变（ΔH°＝-30．513 kJ·mol-1）和熵变（ΔS°＝177．99 J·mol-1·K-1）值表明，氢键与疏水作用是赤藓红与 HSA 相互作用的主要驱动力；紫外和 CD 光谱分析揭示，赤藓红与 HSA 结合引起α-螺旋和无规卷曲含量减少，β-折叠和β-转角含量增加，导致 HSA 的多肽链发生了部分伸展。
재생리산도（pH 7．4）조건하，응용형광광보법、자외-가견흡수광보법화원이색보법（CD）연구료적선홍여인혈청백단백（HSA）적상호작용급기대 HSA 결구적영향。형광적정실험결과표명，정태졸멸시도치 HSA 내원형광졸멸적주요원인；위점경쟁실험현시，적선홍주요결합재 HSA 적아결구역 IIA（site I）；계산출적열역학삼수함변（ΔH°＝-30．513 kJ·mol-1）화적변（ΔS°＝177．99 J·mol-1·K-1）치표명，경건여소수작용시적선홍여 HSA 상호작용적주요구동력；자외화 CD 광보분석게시，적선홍여 HSA 결합인기α-라선화무규권곡함량감소，β-절첩화β-전각함량증가，도치 HSA 적다태련발생료부분신전。
The interactions between a food colorant,erythrosine B (ErB) and human serum albumin (HSA),as well as the effect of the colorant on the protein structure in simulative physiological buffer (pH 7.4)were investigated by fluorescence,UV-vis absorption and circular dichroism (CD)spectroscopy.The result of fluorescence titration suggested that the fluorescence quenching of HSA by ErB was a static quenching procedure.The binding site for ErB on HSA was mainly located in subdomain IIA (site I)of HSA via the site marker competitive experiments.The values of enthalpy change (ΔH°=-30.513 kJ· mol-1 )and entropy change (ΔS°=177.99 J·mol-1 ·K-1 )were calculated via van't Hoff equation,which indicated that the interaction was driven mainly by hydrophobic and hydrogen bonds.Furthermore,the re-sults of UV-vis absorption and CD analysis demonstrated that the addition of ErB resulted in a partial un-folding of the polypeptides of HSA with reduction in α-helix and random coil and increases inβ-sheet andβ-turn structures.