In vitro DNA binding studies of Aspartame, an artificial sweetener

被引:47
作者
Kashanian, Soheila [1 ,2 ]
Khodaei, Mohammad Mehdi [1 ,2 ]
Kheirdoosh, Fahimeh [3 ]
机构
[1] Razi Univ, SBRC, Fac Chem, Kermanshah, Iran
[2] Razi Univ, NNRC, Kermanshah, Iran
[3] Razi Univ, Dept Appl Chem, Fac Chem, Kermanshah, Iran
关键词
CT-DNA interaction; Artificial sweeteners; Aspartame (APM); Groove binding; CALF THYMUS DNA; NUCLEIC-ACIDS; NICKEL(II) COMPLEXES; ETHIDIUM BROMIDE; SPERM DNA; FLUORESCENCE; CLEAVAGE; HOECHST-33258; COBALT(II); SPECTRA;
D O I
10.1016/j.jphotobiol.2013.01.001
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
A number of small molecules bind directly and selectively to DNA, by inhibiting replication, transcription or topoisomerase activity. In this work the interaction of native calf thymus DNA (CT-DNA) with Aspartame (APM), an artificial sweeteners was studied at physiological pH. DNA binding study of APM is useful to understand APM-DNA interaction mechanism and to provide guidance for the application and design of new and safer artificial sweeteners. The interaction was investigated using spectrophotometric, spectrofluorometric competition experiment and circular dichroism (CD). Hypochromism and red shift are shown in UV absorption band of APM. A strong fluorescence quenching reaction of DNA to APM was observed and the binding constants (K-f) of DNA with APM and corresponding number of binding sites (n) were calculated at different temperatures. Thermodynamic parameters, enthalpy changes (Delta H) and entropy changes (Delta S) were calculated to be +181 kJ mol(-1) and +681 J mol(-1) K-1 according to Van't Hoff equation, which indicated that reaction is predominantly entropically driven. Moreover, spectrofluorometric competition experiment and circular dichroism (CD) results are indicative of non-intercalative DNA binding nature of APM. We suggest that APM interacts with calf thymus DNA via groove binding mode with an intrinsic binding constant of 5 x 10(+4) M-1. (C) 2013 Elsevier B.V. All rights reserved.
引用
收藏
页码:104 / 110
页数:7
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