Spectroscopic and molecular modeling study of cyanine dye interacting with human serum transferrin

Zhang, Xiufeng; Chen, Lei; Yang, Qianfan; Li, Qian; Sun, Xin; Chen, Hongbo; Yang, Guang; Tang, Yalin

doi:10.1016/j.colsurfa.2015.01.023

Cited by 13 publications

(1 citation statement)

References 33 publications

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“…The mechanisms of interaction between the anionic meso -substituted trimethine cyanine 52 and human transferrin, as well as conformational changes in the protein, were studied in [ 98 ]. Transferrin (hTf) is a protein whose function is to control the amount of free iron in the blood plasma.…”

Section: Influence Of Interaction With Proteins and Other Biomolecule...mentioning

confidence: 99%

Photonics of Trimethine Cyanine Dyes as Probes for Biomolecules

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Татиколов

2022

Molecules

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Cyanine dyes are widely used as fluorescent probes in biophysics and medical biochemistry due to their unique photophysical and photochemical properties (their photonics). This review is focused on a subclass of the most widespread and studied cyanine dyes—trimethine cyanines, which can serve as potential probes for biomolecules. The works devoted to the study of the noncovalent interaction of trimethine cyanine dyes with biomolecules and changing the properties of these dyes upon the interaction are reviewed. In addition to the spectral-fluorescent properties, elementary photochemical properties of trimethine cyanines are considered, including: photoisomerization and back isomerization of the photoisomer, generation and decay of the triplet state, and its quenching by oxygen and other quenchers. The influence of DNA and other nucleic acids, proteins, and other biomolecules on these properties is covered. The interaction of a monomer dye molecule with a biomolecule usually leads to a fluorescence growth, damping of photoisomerization (if any), and an increase in intersystem crossing to the triplet state. Sometimes aggregation of dye molecules on biomolecules is observed. Quenching of the dye triplet state in a complex with biomolecules by molecular oxygen usually occurs with a rate constant much lower than the diffusion limit with allowance for the spin-statistical factor 1/9. The practical application of trimethine cyanines in biophysics and (medical) biochemistry is also considered. In conclusion, the prospects for further studies on the cyanine dye–biomolecule system and the development of new effective dye probes (including probes of a new type) for biomolecules are discussed.

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Section: Influence Of Interaction With Proteins and Other Biomolecule...mentioning

confidence: 99%

Photonics of Trimethine Cyanine Dyes as Probes for Biomolecules

Пронкин

Татиколов

2022

Molecules

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A Spectroscopic Study of the Interaction between Cyanine Dyes with Different Skeleton Structures and Transferrin

et al. 2018

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Human serum transferrin (hTf) has been exploited as a biocarrier for targeted drugs to cancer cells where transferrin receptors are expressed at high levels. In this study, cyanine dyes DMSA and DMSB with a similar main core structure were selected to evaluate the effects of heterocycle on binding with hTf by spectroscopic methods. Fluorescence spectral results have shown that DMSB, which contains a selenazole ring, had a strong affinity binding with transferrin, up to 10 4 -fold higher than DMSA, which contains a thiazole ring. This difference may be attributed to the larger molecular volume of selenazole compared with DMSA. Binding distance between cyanine dyes and hTf demonstrated that the non-radioactive energy transfer mechanism was also involved in the fluorescence quenching of protein. Furthermore, DMSB-binding gave rise to a greater decrease of the α-helix content of hTf than DMSA suggesting that hTf, which shows a looser structure binding with DMSB, increased polarity around the tryptophan residues of hTf, which was confirmed by circular dichroism and synchronous fluorescence spectroscopy. The study provides a certain theoretical basis for the design of cyanine dyes as biomolecular probe to target drugs for hTf.

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