Interaction between a cationic porphyrin and bovine serum albumin studied by surface plasmon resonance, fluorescence spectroscopy and cyclic voltammetry

Xiao, Chang-Qing; Jiang, Feng-Lei; Zhou, Bo; Li, Ran; Liu, Yi

doi:10.1039/c1pp05008g

Cited by 49 publications

(27 citation statements)

References 23 publications

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“…The K SV values tended to decrease with an increase in temperature (Table ), indicating that the fluorescence quenching mechanism of BPO by ctDNA may be a static quenching . Moreover, the calculated K q values for BPO–ctDNA complex were in the order of 10 12 L mol −1 sec −1 , which were greater than the reported maximum scatter collision‐quenching constant of 2.0 × 10 10 L mol −1 sec −1 for various quenchers with a biopolymer . This result confirmed the static quenching procedure in the BPO–ctDNA interaction.…”

Section: Resultssupporting

confidence: 67%

Deciphering the intercalative binding modes of benzoyl peroxide with calf thymus DNA

2017

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The binding of benzoyl peroxide (BPO), a flour brightener, with calf thymus DNA (ctDNA) was predicted by molecular simulation, and this were confirmed using multi-spectroscopic techniques and a chemometrics algorithm. The molecular docking result showed that BPO could insert into the base pairs of ctDNA, and the adenine bases were the preferential binding sites which were validated by the analysis of Fourier transform infrared spectra. The mode of binding of BPO with ctDNA was an intercalation as supported by the results from ctDNA melting and viscosity measurements, iodide quenching effects and competitive binding investigations. The circular dichroism and DNA cleavage assays indicated that BPO induced a conformational change from B-like DNA structure towards to A-like form, but did not lead to significant damage in the DNA. The complexation was driven mainly by hydrogen bonds and hydrophobic interactions. Moreover, the ultraviolet-visible (UV-vis) spectroscopic data matrix was resolved by a multivariate curve resolution-alternating least-squares algorithm. The equilibrium concentration profiles for the components (BPO, ctDNA and BPO-ctDNA complex) were extracted from the highly overlapping composite response to quantitatively monitor the BPO-ctDNA interaction. This study has provided insights into the mechanism of the interaction of BPO with ctDNA and potential hazards of the food additive.

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Section: Resultssupporting

confidence: 67%

Deciphering the intercalative binding modes of benzoyl peroxide with calf thymus DNA

2017

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“…Generally, the fluorescence emission intensity of the protein is quenched regularly by addition of surfactant-cobalt(III) complexes, indicating the efficient formation of a complex between protein and surfactant-metal complexes. 29 The obtained results were analysed through equations (S4) and (S5) † and the values for K sv , k q , K b and n are summarized in Table 2.…”

Section: Analysis Of Quenching and Binding Parametersmentioning

confidence: 99%

Study of single and double chain surfactant–cobalt(iii) complexes and their hydrophobicity, micelle formation, interaction with serum albumins and antibacterial activities

Veeralakshmi

Nehru

Arunachalam

et al. 2014

Inorg. Chem. Front.

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To develop surfactant based metallodrugs, it is important to know the role of the tail part of the surfactant-metal complexes in their hydrophobicity, micellization behaviour, interaction with biomacromolecules and cell penetration. Here, we have taken a new series of single and double chain surfactant-cobalt(III) complexes with alkylamine ligands of different chain length, [Co(dien)(DA)Cl 2 ]ClO 4 (1), [Co(dien)(HA)-Cl 2 ]ClO 4 (2), [Co(dien)(DA) 2 Cl](ClO 4 ) 2 (3) and [Co(dien)(HA) 2 Cl](ClO4) 2 (4), where dien = diethylenetriamine, DA = dodecylamine and HA = hexadecylamine. The complexes were characterised by elemental analysis, NMR, ESI-MS, UV-visible and FTIR techniques. In addition, the average size distribution and morphology of self-assembled surfactant-cobalt(III) complexes were examined by DLS and SEM, respectively.The hydrophobicity, critical micelle concentration (CMC) values, thermodynamics of micellization (ΔG°m, ΔH°m and ΔS°m) and the nature of the interaction of these complexes with bovine and human serum albumins (BSA/HSA) were evaluated. The obtained CMC values were in the order 1 > 2 > 3 > 4, indicating that double chain systems have lower CMC values compared to single chain systems due to the increase in the hydrophobicity of the alkyl amine ligands. The thermodynamics of micellization indicated that the process is spontaneous, exothermic and entropy driven. The interaction of complexes 1-4 with serum albumins indicated that the quenching process follows a static mechanism, and the extent of quenching and binding parameters were in the order 1 < 2 < 3 < 4. Interestingly, on increasing the temperature, the protein-complex stability decreased for the single chain systems, and increased for the double chain systems, probably due to the involvement of electrostatic and hydrophobic interactions. This was further supported by the thermodynamics of protein interaction and synchronous fluorescence studies. Moreover, the results from UV-vis, synchronous and circular dichroism (CD) showed the occurrence of conformational and micro environmental changes in BSA/HSA. It is also noted that BSA has more binding affinity with surfactant-metal complexes compared to HSA. Furthermore, the antimicrobial effects of these complexes were investigated by disk diffusion method; complex 4 has a better antimicrobial activity due to the ease of bacterial cell penetration due to its more hydrophobic nature.

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“…2B) showed a good linearity and the K SV values decreased with increasing temperature ( Table 1), suggesting that the fluorescence quenching mechanism may be static quenching. Moreover, K q values (1.31 Â 10 12 , 0.73 Â 10 12 , 0.65 Â 10 12 and 0.62 Â 10 12 L mol À1 s À1 at 292, 298, 304 and 310 K, respectively) were higher than the maximum scatter collision-quenching constant for various quenchers with biopolymers, 2.0 Â 10 10 L mol À1 s À1 , indicating that static quenching was the probable quenching mechanism of PSO-trypsin interaction [31,32].…”

Section: Fluorescence Spectra Studiesmentioning

confidence: 86%

Binding characteristics of psoralen with trypsin: Insights from spectroscopic and molecular modeling studies

Liu

Zhang

Liao

et al. 2015

Spectrochimica Acta Part A: Molecular and Biomolecular Spectros

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Interaction between a cationic porphyrin and bovine serum albumin studied by surface plasmon resonance, fluorescence spectroscopy and cyclic voltammetry

Cited by 49 publications

References 23 publications

Deciphering the intercalative binding modes of benzoyl peroxide with calf thymus DNA

Deciphering the intercalative binding modes of benzoyl peroxide with calf thymus DNA

Study of single and double chain surfactant–cobalt(iii) complexes and their hydrophobicity, micelle formation, interaction with serum albumins and antibacterial activities

Binding characteristics of psoralen with trypsin: Insights from spectroscopic and molecular modeling studies

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