应用化工
應用化工
응용화공
APPLIED CHEMICAL INDUSTRY
2014年
9期
1728-1733
,共6页
王志宏%彭胜%周云雷%郑阳%史丽娟%彭密军
王誌宏%彭勝%週雲雷%鄭暘%史麗娟%彭密軍
왕지굉%팽성%주운뢰%정양%사려연%팽밀군
杜仲%绿原酸%牛血清白蛋白%金属离子%荧光猝灭
杜仲%綠原痠%牛血清白蛋白%金屬離子%熒光猝滅
두중%록원산%우혈청백단백%금속리자%형광졸멸
Eucommia ulmoides Oliv.%chlorogenic acid%bovine serum albumin%heavy metal%fluores-cence quenching
以杜仲绿原酸(CA)为原料,在模拟人体生理条件下,采用荧光光谱和紫外吸收光谱等方法,考察 Cu2+、Zn2+和 Pb2+对 CA 与牛血清白蛋白(BSA)相互作用产生的影响。结果表明,金属离子的存在不会改变 CA 对 BSA的猝灭类型,但对其猝灭速率常数(kq )、结合常数(K)以及结合位点(n)会有不同程度的影响;CA 与 BSA 之间的反应属于自发型,主要以范德华力和氢键为主,Zn2+和 Pb2+的存在不会改变其作用力类型,Cu2+则会使作用力变为以静电吸引力为主;Zn2+和 Pb2+会将供体与受体之间的结合距离分别减小1.975%和14.07%,Cu2+的干扰使CA 与 BSA 之间的结合距离增大11.58%;同步荧光光谱显示 CA 与 BSA 中的酪氨酸残基和色氨酸残基都有相互作用,三维荧光测定结果进一步表明猝灭剂对 BSA 构象及微环境会引起变化。
以杜仲綠原痠(CA)為原料,在模擬人體生理條件下,採用熒光光譜和紫外吸收光譜等方法,攷察 Cu2+、Zn2+和 Pb2+對 CA 與牛血清白蛋白(BSA)相互作用產生的影響。結果錶明,金屬離子的存在不會改變 CA 對 BSA的猝滅類型,但對其猝滅速率常數(kq )、結閤常數(K)以及結閤位點(n)會有不同程度的影響;CA 與 BSA 之間的反應屬于自髮型,主要以範德華力和氫鍵為主,Zn2+和 Pb2+的存在不會改變其作用力類型,Cu2+則會使作用力變為以靜電吸引力為主;Zn2+和 Pb2+會將供體與受體之間的結閤距離分彆減小1.975%和14.07%,Cu2+的榦擾使CA 與 BSA 之間的結閤距離增大11.58%;同步熒光光譜顯示 CA 與 BSA 中的酪氨痠殘基和色氨痠殘基都有相互作用,三維熒光測定結果進一步錶明猝滅劑對 BSA 構象及微環境會引起變化。
이두중록원산(CA)위원료,재모의인체생리조건하,채용형광광보화자외흡수광보등방법,고찰 Cu2+、Zn2+화 Pb2+대 CA 여우혈청백단백(BSA)상호작용산생적영향。결과표명,금속리자적존재불회개변 CA 대 BSA적졸멸류형,단대기졸멸속솔상수(kq )、결합상수(K)이급결합위점(n)회유불동정도적영향;CA 여 BSA 지간적반응속우자발형,주요이범덕화력화경건위주,Zn2+화 Pb2+적존재불회개변기작용력류형,Cu2+칙회사작용력변위이정전흡인력위주;Zn2+화 Pb2+회장공체여수체지간적결합거리분별감소1.975%화14.07%,Cu2+적간우사CA 여 BSA 지간적결합거리증대11.58%;동보형광광보현시 CA 여 BSA 중적락안산잔기화색안산잔기도유상호작용,삼유형광측정결과진일보표명졸멸제대 BSA 구상급미배경회인기변화。
Interaction of chlorogenic acid(CA)from Eucommia ulmoides Oliv. with bovine serum albumin (BSA)was explored under simulative physiological conditions accompany with fluorescence spectroscopy and UV-Vis absorption in the absence and presence of Cu2 + ,Zn2 + and Pb2 + . The results indicated that the mold of fluorescence quenching of CA to BSA was not changed in the presence metal ions,but the quenching rate constant(kq ),the binding constants(K)and binding sites(n)were changed in different degrees. The interaction between of CA and BSA was spontaneous and van der waals force together with hydrogen bond played important roles in this binding process,at the same time,the type was not changed in the presence of Zn2 + and Pb2 + . But electrostatic interaction was not negligible in presence of Cu2 + , Zn2 + and Pb2 + decreased the binding distance of CA for BSA by 1. 975% and 14. 07% ,respectively. However,Cu2 + increased the binding distance of CA for BSA by 11. 58% . Interactions of the tryptophan and tyrosine residues with CA have been discovered by synchronous fluorescence spectroscopic. The re-sults of three-dimensional fluorescence spectroscopy revealed that the conformational and micro-environ-ment of BSA were changed owing to the presence of quencher.