Spectroscopic Investigation on the Binding of a Cyanine Dye with Transferrin

Zhang, Xiufeng; Ling, Lan; Chen, Lei; Chen, Hongbo; Yang, Qianfan; Li, Qian; Li, Qi-long; Sun, Xin; Tang, Yalin

doi:10.1002/poc.3508

Cited by 11 publications

(2 citation statements)

References 34 publications

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“…When Δλ = 60 nm, a blue shift (from 281 to 276 nm) and a decrease in the synchronous fluorescence intensity of Trp are observed by increasing the concentration of the Fe complex, which indicated that the polarity around the Trp residues decreased and the hydrophobicity increased. [ 42 ]…”

Section: Resultsmentioning

confidence: 99%

A multidisciplinary study for investigating the interaction of an iron complex with bovine liver catalase

Hashemizadeh

Shiri

Shahraki

et al. 2022

Applied Organom Chemis

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Catalase (CAT) is an essential protein protecting the cell from oxidative damage by reactive oxygen species. CAT is a heme enzyme in which iron metal plays a crucial role in catalytic activity. In this research, an iron (II, III) complex ([Fe (bpy) 3 ] [Fe (dipic) 2 ] 2 .7H 2 O; dipic À2 = pyridine-2,6-dicarboxylato and bpy = 2,2 0 -bipyridine) was used to evaluate its binding interactions with bovine liver catalase (BLC) using spectroscopic and molecular docking methods. The experimental results demonstrated that the catalytic activity of BLC increased slightly and reached 106% of the initial activity. The interactions between Fe complex and BLC led to the quenching of the catalase fluorescence emission via the static quenching mechanism. Thermodynamic parameters demonstrated that the predominant interactions between catalase and Fe complex are hydrogen bond and van der Waals and the process is exothermic and enthalpy driven. The circular dichroism (CD) and synchronous fluorescence results showed that the Fe complex altered the structure and conformation of BLC. It changed the secondary structure of BLC by decreasing α-helix and β-sheet content. Also, the experimental data were analyzed using Multivariate Curve Resolution-Alternating Least Square (MCR-ALS) to the resolution of measured complex spectra and estimate the number of independent chemical species. The docking results in agreement with experimental data showed that the cationic part of the complex with catalase is mainly hydrophobic and van der Waals interactions, and for the anionic part are hydrophobic, van der Waals, and hydrogen bonding.

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Section: Resultsmentioning

confidence: 99%

A multidisciplinary study for investigating the interaction of an iron complex with bovine liver catalase

Hashemizadeh

Shiri

Shahraki

et al. 2022

Applied Organom Chemis

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“…Binding of dye 52 occurs in the N-lobe of the protein and leads to an increase in the content of α-helices and increased hydrophobicity around tryptophan residues of hTf. Spectral-fluorescent and CD spectroscopies as well as molecular modeling have been used to study the binding mechanisms of dye 53 to hTf at various pH and temperatures [ 99 ]. As well as being structurally similar to 52 , trimethine cyanine 53 binds to hTf in the N-lobe with a high K eff ~10 7 L mol −1 ; quenching of intrinsic fluorescence of hTf by the dye is observed.…”

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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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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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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Spectroscopic Investigation on the Binding of a Cyanine Dye with Transferrin

Cited by 11 publications

References 34 publications

A multidisciplinary study for investigating the interaction of an iron complex with bovine liver catalase

A multidisciplinary study for investigating the interaction of an iron complex with bovine liver catalase

Photonics of Trimethine Cyanine Dyes as Probes for Biomolecules

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

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