Folic acid complexes with human and bovine serum albumins

Bourassa, P.; Hasni, Imed; Tajmir-Riahi, H.A.

doi:10.1016/j.foodchem.2011.05.094

Cited by 147 publications

(63 citation statements)

References 38 publications

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“…However, the absorbance intensity for BSA was higher than that for the FA-BSA mixture at each concentration. This difference in absorbance is a result of the quenching effect of FA molecules on BSA, as reported in the literature [16].…”

Section: Resultssupporting

confidence: 67%

“…Therefore, BSA forms a blue dye-BSA complex that can be detected by a UV-Vis spectrophotometer at 595 nm [22]. However, FA and BSA also form complexes with each other [16,17]. Note that dye-BSA complexes continue to form even after FA-BSA association (as recorded in the spectrographs shown in Fig.…”

Section: Resultsmentioning

confidence: 86%

“…FA forms complexes with proteins such as bovine serum albumin (BSA) and human serum albumin (HSA) [16] due to electrostatic forces and hydrogen bonding [17]. Most of the studies focused to increase the bioavailability of FA and used spectroscopic techniques to probe the interactions between FA and BSA.…”

Section: Introductionmentioning

confidence: 99%

“…Most of the studies focused to increase the bioavailability of FA and used spectroscopic techniques to probe the interactions between FA and BSA. According to the literature, tryptophan (Trp) can be involved in FA-protein associations [16,17]. Moreover, Trp itself forms a complex with FA [18].…”

Section: Introductionmentioning

confidence: 99%

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An investigation of folic acid–protein association sites and the effect of this association on folic acid self-assembly

et al. 2015

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The contribution of folic acid (FA)-tryptophan interactions to FA-protein association was investigated in the context of using FA as a drug carrier in protein delivery systems. Bovine serum albumin (BSA) and indolicidin were used as model proteins in the study. The FA-BSA complex was characterized by using the Bradford reagent to identify the impact of FA-BSA association on BSA-dye reagent interactions. UV-visible spectroscopic analysis of the FA-BSA mixture showed that the absorbance maximum of BSA-dye reagent occurred at 595 nm, even after the association of FA with BSA. This confirms that protonated amino acid groups of the protein are not involved in FA-BSA association. Moreover, molecular dynamics (MD) simulation confirmed the presence of an associative interaction between aromatic moieties in FA and tryptophan moieties in the indolicidin molecule, which disrupted FA self-assembly. An X-ray diffraction (XRD) study showed that there was limited disruption of FA self-assembly after the addition of BSA or tryptophan. This suggests that FA and BSA are compatible and associate with each other. Graphical Abstract Mechanism of folic acid and protein association.

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Section: Resultssupporting

confidence: 67%

Section: Resultsmentioning

confidence: 86%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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An investigation of folic acid–protein association sites and the effect of this association on folic acid self-assembly

et al. 2015

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“…Thus, HSA is able to increase the in vivo half-life and water solubility of drugs. The deeper knowledge of the binding ability of a drug to the non-specific transporter protein HSA becomes an important research field in chemistry, biochemistry and clinical medicine and screening of the binding to blood proteins is required by the FDA for a potential therapeutic agent [3][4][5][6].…”

Section: Introductionmentioning

confidence: 99%

Interaction of anticancer reduced Schiff base coumarin derivatives with human serum albumin investigated by fluorescence quenching and molecular modeling

Dömötör

Tuccinardi

Karcz

et al. 2014

Bioorganic Chemistry

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The specific binding of five reduced Schiff base derived 7-amino-coumarin compounds with antitumor activity to human serum albumin, the principal binding protein of blood, was studied by fluorescence spectroscopy. Their conditional binding constants were computed and the reversible binding at the Sudlow's site I was found to be strong (K D ~ 0.03-2.09 M).Based on the data albumin can provide a depot for the compounds and is responsible for their biodistribution and transport processes. The experimental data is complemented by proteinligand docking calculations for two representatives which support the observations. The proton dissociation constants of the compounds were also determined by UV-Vis spectrophotometric and fluorometric titrations to obtain the actual charges and distribution of the species in the various protonation states at physiological pH.

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Low molecular weight chitosan oligosaccharides form stable complexes with human lactoferrin

Li,

Guan,

Cai

et al. 2023

FEBS Open Bio

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Proteins in tears, including human lactoferrin (HLF), can be deposited and denatured on contact lenses, increasing the risk of microbial cell attachment to the lens and ocular complications. The surfactants currently used in commercial contact lens care solutions have low clearance ability for tear proteins. Chitosan oligosaccharide (COS) binds to a variety of proteins, and has potential for use in protein removal, especially in contact lens care solutions. Here, we analyzed the interaction mechanism of COSs hydrolyzed from chitosan from different resources with HLF. The molecular weights (MWs) and concentrations of COSs were key factors for the formation of COS‐HLF complexes. Lower MWs of COSs could form more stable COS‐HLF complexes. COS from Aspergillus ochraceus had a superior effect on HLF compared with COS from shrimp and crab shell with the same MWs. In conclusion, COSs could bind to and cause a conformational change in HLF. Therefore, COSs, especially those with low MWs, have potential as deproteinizing agents in contact lens care solution.

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Folic acid complexes with human and bovine serum albumins

Cited by 147 publications

References 38 publications

An investigation of folic acid–protein association sites and the effect of this association on folic acid self-assembly

An investigation of folic acid–protein association sites and the effect of this association on folic acid self-assembly

Interaction of anticancer reduced Schiff base coumarin derivatives with human serum albumin investigated by fluorescence quenching and molecular modeling

Low molecular weight chitosan oligosaccharides form stable complexes with human lactoferrin

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