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Schiff 碱-N,N'-双(水杨醛)反式-1,2-二氨基环己烷在蛋白质和胶束环境中的荧光行为。

Fluorescence Behavior of Schiff Base-N, N'-bis(salicylidene) Trans 1, 2-Diaminocyclohexane in Proteinous and Micellar Environments.

机构信息

Department of Chemistry, Assam University, Silchar, Assam, 788 011, India.

出版信息

J Fluoresc. 2017 Nov;27(6):2295-2311. doi: 10.1007/s10895-017-2171-6. Epub 2017 Aug 22.

DOI:10.1007/s10895-017-2171-6
PMID:28831629
Abstract

Fluorescence properties of N, N'-bis(salicylidene) trans 1, 2-diaminocyclohexane (H L) is used to probe the anionic (SDS), cationic (CTAB) and nonionic (TX-100) micelles as well as in serum albumins (BSA and HSA) and chicken egg white lysozyme (LYZ) by steady state and picosecond time-resolved fluorescence spectroscopy. The fluorescence band intensity was found to increase with concomitant blue-shift with gradual addition of different surfactants. All the experimental results suggest that the probe molecule resides in the micelle-water interface rather than going into the micellar core. However, the penetration is more towards the micellar hydrocarbon core in nonionic surfactant (TX-100) while comparing with ionic surfactants (SDS and CTAB). Several mean microscopic properties such as critical micelle concentration, polarity parameters and binding constant were calculated in presence of different surfactants. The decrease in nonradiative decay rate constants in micellar environments indicates restricted motion of the probe inside the micellar nanocages with increasing fluorescence emission intensity and quantum yields. Further in this work, we also investigated the interaction behavior of the probe with different proteins at low concentrations under physiological conditions (pH = 7.4). Stern-Volmer analysis of the tryptophan (Trp) fluorescence quenching data in presence of probe reveals Stern-Volmer constant (K) as well as bimolecular quenching rate constant (K). The binding constant as well as the number of binding sites of the probe with proteins were also monitored and found to be 1:1 stoichiometry ratio.

摘要

N,N'-双(水杨醛)反式-1,2-二氨基环己烷(HL)的荧光性质用于通过稳态和皮秒时间分辨荧光光谱法探测阴离子(SDS)、阳离子(CTAB)和非离子(TX-100)胶束以及血清白蛋白(BSA 和 HSA)和鸡卵清白溶菌酶(LYZ)。发现荧光带强度随着不同表面活性剂的逐渐加入而增加,同时伴有蓝移。所有实验结果表明,探针分子位于胶束-水界面,而不是进入胶束核心。然而,与离子表面活性剂(SDS 和 CTAB)相比,探针分子在非离子表面活性剂(TX-100)中更倾向于进入胶束烃核。在存在不同表面活性剂的情况下,计算了几个平均微观性质,如临界胶束浓度、极性参数和结合常数。在胶束环境中,非辐射衰减速率常数的降低表明探针在胶束纳米笼内的运动受到限制,同时荧光发射强度和量子产率增加。在这项工作中,我们还在生理条件(pH=7.4)下,在低浓度下研究了探针与不同蛋白质的相互作用行为。在存在探针的情况下,色氨酸(Trp)荧光猝灭数据的斯特恩-沃尔默分析揭示了斯特恩-沃尔默常数(K)和双分子猝灭速率常数(K)。还监测了探针与蛋白质的结合常数和结合位点数量,并发现为 1:1 化学计量比。

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