期刊
JOURNAL OF BIOMOLECULAR STRUCTURE & DYNAMICS
卷 40, 期 17, 页码 7779-7785出版社
TAYLOR & FRANCIS INC
DOI: 10.1080/07391102.2021.1902397
关键词
Methylene blue; DNA; human serum albumin; absorption and fluorescence spectra; denaturation curve
The study on the interaction of thiazine dye methylene blue (MB) with DNA and albumin revealed that MB stabilizes the native structure of these biomolecules, increasing the melting temperature of the complexes. MB binds to DNA by intercalation and electrostatic mechanisms, while the main binding mode with albumin is electrostatic, leading to protein stabilization.
The interaction of thiazine dye methylene blue (MB) with Calf thymus DNA and human blood serum albumin (HSA) has been studied. MB was revealed to stabilize the native structure of DNA and HSA, since the melting temperature of the complexes is shifted to higher values in relation to that of both macromolecules in pure state. It was also revealed that the absorption and fluorescence spectra of the MB-DNA complexes change significantly, while those of MB-albumin complexes do not change noticeably. Analysis of the obtained data allows to conclude that MB binds to DNA by two modes, including intercalation and electrostatic mechanisms. In the case of HSA, the main binding mode of MB, conditioning the stabilization of the protein native structure, is the electrostatic mechanism. Communicated by Ramaswamy H. Sarma
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