Spectroscopic characterization of the binding mechanism of fluorescein and carboxyfluorescein in human serum albumin

Sulaiman, Saba A. J.; Kulathunga, H. Udani; Abou‐Zied, Osama K.

doi:10.1117/12.2077520

Cited by 3 publications

(2 citation statements)

References 33 publications

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“…Normally, the static quenching process is characterized by the formation of complexes. [ 44 ] Figure 10 showed the UV‐Vis spectra of N‐CDs and HSA. Due to C = O and amino acid residues in HSA, there were two intrinsic absorption peaks at 225 and 280 nm, respectively.…”

Section: Resultsmentioning

confidence: 99%

Spectroscopic cyclic voltammetry, and molecular docking study on the molecular interaction between synthesized blue emitting nitrogen‐doped carbon dots and human serum albumin

et al. 2021

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Fluorescent carbon dots are a promising drug carrier and bio‐sensor material. The study between human serum albumin and carbon dots could explore the possible interaction mechanism. In this paper, melamine was adopted as passivating agent and citric acid as carbon source, high fluorescence nitrogen doped carbon dots (N‐CDs) were synthetized by one‐pot solid phase pyrolysis successfully. The obtained blue emissive N‐CDs with an average particle size of 2.8 ± 0.7 nm displayed an excitation‐dependent photoluminescence behavior, and the fluorescence quantum yield was estimated to be 12.8%. Moreover, the N‐CDs contained abundant hydroxyl, carboxyl, and amine groups. The molecular interaction between as‐prepared N‐CDs and HSA was systematically investigated in vitro through several spectroscopic methods associated with cyclic voltammetry (CV) and molecular docking. The quenching mechanism of HSA by N‐CDs was static through forming the HSA‐N‐CDs complex, and both hydrogen bonding and van der Waals forces were the fundamental driving forces in the spontaneous binding process. The distance between N‐CDs and HSA was 2.2 nm on the basis of Förster's theory. The competitive binding experiment showed that the binding of N‐CDs was primarily in site I of HSA. Through the analysis of circular dichroism (CD), synchronous fluorescence, and three‐dimensional fluorescence spectra, the secondary structure of HSA was altered in the presence of N‐CDs and the polarity around the amino acid residues of HSA was not changed. Besides, molecular simulation was applied to determine the possible binding situation. Our study explored the interaction mechanism of N‐CDs with HSA, which provided some valuable information for understanding the structure and function of proteins as well as the transport and metabolism of N‐CDs.

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Section: Resultsmentioning

confidence: 99%

Spectroscopic cyclic voltammetry, and molecular docking study on the molecular interaction between synthesized blue emitting nitrogen‐doped carbon dots and human serum albumin

et al. 2021

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“…Generally, static quenching will lead to change in UV–vis spectrum intensity, but dynamic quenching will not. [ 17 ] In Figure 6, we can see that hyperoside produces UV absorption at 250 nm–300 nm and overlaps that of HSA. Therefore, we measured the quenching spectra of HSA and hyperoside using an absorbance subtraction method.…”

Section: Resultsmentioning

confidence: 99%

Study on the interaction of hyperoside and human serum albumin in V_C and V_C‐free environments by spectroscopic and molecular docking techniques

Xin

Chen

et al. 2020

Luminescence

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The interaction between hyperoside and human serum albumin was studied in vitamin C (VC) and VC‐free environments using ultraviolet (UV)–vis absorption, fluorescence, circular dichroism spectra, and molecular docking techniques under simulated physiological conditions. The two environments had different influences on the secondary structure of human serum albumin (HSA). The α‐helix content was slightly increased from 50% to 51% in the VC environment and increased from 50% to 55% in the VC‐free environment. The thermodynamic parameters were ΔH° = −30.7 kJ⋅mol−1 and ΔS° = −23.4 mol−1⋅K−1 in the VC environment and ΔH° = −25.4 kJ⋅mol−1 and ΔS° = −11.4 J⋅mol−1⋅K−1 in the VC‐free environment. Through thermodynamics parameters, hydrophobic force played a dominant role in the whole environment. The binding constants were calculated to be 7.25 × 105 mol⋅L−1 and 9.76 × 105 mol⋅L−1 at 298 K and they declined with the rise in temperature. The two binding distances were 2.6 nm and 2.5 nm respectively at 298 K, indicating that fluorescence energy transfer occurred. The UV–vis spectra indicated that fluorescence quenching of the HSA–hyperoside complex was a static quenching process. Hyperoside could spontaneously bind to HSA at site I (subdomain IIA). Molecular docking elucidated the way to binding basically through hydrophobic and van der Waals force interactions. Moreover, molecular docking showed that the VC environment could influence binding of HSA and hyperoside by more H‐binding and less hydrophobic forces.

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Study on the binding interaction and stability of whey protein concentrate-80 with folic acid

Wang,

Tang

et al. 2024

Colloids and Surfaces A: Physicochemical and Engineering Aspect

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Spectroscopic characterization of the binding mechanism of fluorescein and carboxyfluorescein in human serum albumin

Cited by 3 publications

References 33 publications

Spectroscopic cyclic voltammetry, and molecular docking study on the molecular interaction between synthesized blue emitting nitrogen‐doped carbon dots and human serum albumin

Spectroscopic cyclic voltammetry, and molecular docking study on the molecular interaction between synthesized blue emitting nitrogen‐doped carbon dots and human serum albumin

Study on the interaction of hyperoside and human serum albumin in V_C and V_C‐free environments by spectroscopic and molecular docking techniques

Study on the binding interaction and stability of whey protein concentrate-80 with folic acid

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Spectroscopic characterization of the binding mechanism of fluorescein and carboxyfluorescein in human serum albumin

Cited by 3 publications

References 33 publications

Spectroscopic cyclic voltammetry, and molecular docking study on the molecular interaction between synthesized blue emitting nitrogen‐doped carbon dots and human serum albumin

Spectroscopic cyclic voltammetry, and molecular docking study on the molecular interaction between synthesized blue emitting nitrogen‐doped carbon dots and human serum albumin

Study on the interaction of hyperoside and human serum albumin in VC and VC‐free environments by spectroscopic and molecular docking techniques

Study on the binding interaction and stability of whey protein concentrate-80 with folic acid

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Study on the interaction of hyperoside and human serum albumin in V_C and V_C‐free environments by spectroscopic and molecular docking techniques