CAJ | 학술논문

采用荧光猝灭光谱、紫外-可见吸收光谱研究了桑色素与人血清白蛋白（ HSA）的结合作用。实验表明桑色素对HSA的荧光猝灭属于单一静态猝灭反应，在溶液中以摩尔比1：1牢固结合，各结合反应的平衡常数Kp>105，结合常数Kb>104；根据F?rster非辐射能量转移机理，求算HSA与桑色素间距离r为3.81~3.58nm，能量转移效率E为0.18~0.13。并根据结合反应的热力学常数推测了药物与HSA之间的主要作用力类型为疏水作用力和偶极-偶极作用力。
채용형광졸멸광보、자외-가견흡수광보연구료상색소여인혈청백단백（ HSA）적결합작용。실험표명상색소대HSA적형광졸멸속우단일정태졸멸반응，재용액중이마이비1：1뢰고결합，각결합반응적평형상수Kp>105，결합상수Kb>104；근거F?rster비복사능량전이궤리，구산HSA여상색소간거리r위3.81~3.58nm，능량전이효솔E위0.18~0.13。병근거결합반응적열역학상수추측료약물여HSA지간적주요작용력류형위소수작용력화우겁-우겁작용력。
The interaction of Morin with Human Serum Albumin(HSA) was studied by Spectrometry , UV-visible absorption spectrophotometry and fluorescence spectrometry. The result show that the Morin could induce an endogenous fluorscence quenching of HSA ,which was proved to be a process of static quenching by the fitting equations of Stern-Volmer and double logarithm equation. The binding constants were determined to be more than 104.The binding site(n)was about 1.The binding distance was estimated to be 3.81~3.58nm according to F?rster nonradiation energy transfer mechanism.Energy transfer effciency of E were 0.18~0.13J.The thermodynamic parameters suggested that the interaction forces between Morin and HSA were mainly hydrophobic interaction and dipole-dipole interaction.