Self‐assembly of folic acid in aqueous media

Motkar, Ganesh; Lonare, Manish; Patil, Omkar; Mohanty, Sanat

doi:10.1002/aic.14066

Cited by 24 publications

(26 citation statements)

References 30 publications

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“…Major peaks in the XRD pattern of pure FA occurred at 5.54°, 11.04°, 16.51°, 22.02°, and 27.52°, corresponding to d-spacings of 15.94, 8.05, 5.36, 4.03, and 3.24 Å, respectively. The XRD pattern of FA is similar to the profile given in the literature for FA [21]. All of the major peaks seen for pure FA are retained after the addition of the additive.…”

Section: Xrd Studymentioning

confidence: 74%

“…The impact of varying the protein concentration on the FA-protein complex was investigated using the XRD technique. Previous studies have explained the importance of π-π stacking in the molecular self-assembly of FA using the XRD technique [20,21]. Hence, the results of this study should aid the design of efficient folate nanoparticles for protein delivery.…”

Section: Introductionmentioning

confidence: 82%

“…All of the major peaks seen for pure FA are retained after the addition of the additive. The peak at (2θ =) 21.9°in each spectrum, corresponding to a d-spacing of 4.05 Å, is the signature peak for aromatic ring interactions in FA [21,25]. All peak intensities decrease with increasing concentration of BSA, but they do not disappear within the concentration ranges of interest.…”

Section: Xrd Studymentioning

confidence: 95%

“…This FA stock solution was neutralized to pH 6.5 with 1 M NaOH. FA solution presents liquidcrystalline properties and the color of the solution turns bright yellow after neutralization [21]. BSA stock solution of concentration 1 mg/ml was prepared in water.…”

Section: Methodsmentioning

confidence: 99%

“…This simulation software uses graphics processors for computational calculations [21]. A constant number of molecules were placed in a cubic unit cell at a pressure of 1 bar and a temperature of 298 K (NPT ensemble).…”

Section: Simulation Parametersmentioning

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: Xrd Studymentioning

confidence: 74%

Section: Introductionmentioning

confidence: 82%

Section: Xrd Studymentioning

confidence: 95%

Section: Methodsmentioning

confidence: 99%

Section: Simulation Parametersmentioning

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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An analysis of the interactions between folic acid and aromatic guest molecules

Gupta

Mohanty

2018

J Mol Model

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The formation of complexes between folate and therapeutic drug molecules is well known. In this work, we attempted to elucidate the role of the aromatic rings of folate and drug molecules in interactions between both of these molecules. A detailed molecular simulation study was carried out to explore the associative behavior of folic acid with phenylalanine and tyrosine, which show fluorescence emission following the excitation of these molecules at 257 nm and 274 nm, respectively. Therefore, studies of fluorescence emission from phenylalanine and tyrosine were performed in this work. The results of these studies indicated that folic acid associates with phenylalanine and tyrosine with binding constants ranging from 1.46 × 10 to 2.66 × 10 M. X-ray diffraction studies suggested that folic acid self-assembly is maintained in the presence of associative interactions of the folic acid with guest molecules. These results demonstrate that the aromatic rings in the structures of the folic acid and the therapeutic drug play an important role in the encapsulation of guest molecules through folate self-assembly.

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Sustained release of methotrexate through liquid-crystalline folate nanoparticles

Misra

Mohanty

2014

J Mater Sci: Mater Med

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To make chemotherapy more effective, sustained release of the drug is desirable. By controlling the release rates, constant therapeutic levels can be achieved which can avoid re-administration of drug. This helps to combat tumors more effectively with minimal side effects. The present study reports the control release of methotrexate through liquid-crystalline folate nanoparticles. These nanoparticles are composed of highly ordered folate self-assembly which encapsulate methotrexate molecules. These drug molecules can be released in a controlled manner by disrupting this assembly in the environment of monovalent cations. The ordered structure of folate nanoparticles offers low drug losses of about 4-5%, which is significant in itself. This study reports the size-control method of forming methotrexate encapsulated folate nanoparticles as well as the release of methotrexate through these nanoparticles. It has been demonstrated that methotrexate release rates can be controlled by controlling the size of the nanoparticles, cross-linking cation and cross-linking concentration. The effect of different factors like drug loading, release medium, and pH of the medium on methotrexate release rates was also studied.

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Self‐assembly of folic acid in aqueous media

Cited by 24 publications

References 30 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

An analysis of the interactions between folic acid and aromatic guest molecules

Sustained release of methotrexate through liquid-crystalline folate nanoparticles

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