Stabilization effects of kosmotrope systems on ornithine carbamoyltransferase

Barreca, Davide; Bellocco, Ersilia; Galli, G.; Laganà, Giuseppina; Leuzzi, Ugo; Magazù, Salvatore; Migliardo, F.; Galtieri, Antonio; Telling, Mark

doi:10.1016/j.ijbiomac.2009.04.012

Cited by 14 publications

(2 citation statements)

References 49 publications

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“…The binding of molecules to macromolecules involves mainly non-covalent interactions (such as hydrogen bonds, van der Waals forces, hydrophobic, and electrostatic interactions). These types of forces can be analyzed by determining the thermodynamic parameters of the binding reaction [13,[28][29][30][31][32][33][34][35]. Therefore, the thermodynamic parameters dependent on temperature were calculated from the van't Hoff plot to characterize the forces acting between nitrofurantoin and HSA.…”

Section: Thermodynamics and Acting Forcesmentioning

confidence: 99%

Molecular Basis of Interactions between the Antibiotic Nitrofurantoin and Human Serum Albumin: A Mechanism for the Rapid Drug Blood Transportation

Calderaro

Maugeri

Magazù

et al. 2021

IJMS

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Nitrofurantoin is an antimicrobial agent obtained through the addition of a nitro group and a side chain containing hydantoin to a furan ring. The interactions of the antibiotic with human serum albumin (HSA) have been investigated by fluorescence, UV-VIS, Fourier transform infrared spectroscopy (FTIR) spectroscopy, and protein-ligand docking studies. The fluorescence studies indicate that the binding site of the additive involves modifications of the environment around Trp214 at the level of subdomain IIA. Fluorescence and UV-VIS spectroscopy, displacement studies, and FTIR experiments show the association mode of nitrofurantoin to HSA, suggesting that the primary binding site of the antibiotic is located in Sudlow’s site I. Molecular modeling suggests that nitrofurantoin is involved in the formation of hydrogen bonds with Trp214, Arg218, and Ser454, and is located in the hydrophobic cavity of subdomain IIA. Moreover, the curve-fitting results of the infrared Amide I’ band indicate that the binding of nitrofurantoin induces little change in the protein secondary structure. Overall, these data clarify the blood transportation process of nitrofurantoin and its rapid transfer to the kidney for its elimination, hence leading to a better understanding of its biological effects and being able to design other molecules, based on nitrofurantoin, with a higher biological potential.

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Section: Thermodynamics and Acting Forcesmentioning

confidence: 99%

Molecular Basis of Interactions between the Antibiotic Nitrofurantoin and Human Serum Albumin: A Mechanism for the Rapid Drug Blood Transportation

Calderaro

Maugeri

Magazù

et al. 2021

IJMS

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“…They also tend to increase the thermal stability of proteins and nucleic acids (e.g. (Barreca et al 2009;Coelho et al 2015;de Xammar Oro 2001;Garajová et al 2017;Mashino and Fridovich 1987;Sampedro and Uribe 2004;Wu et al 1993)). Both chaotropic and kosmotropic ions inhibit the growth of Pseudomonas aeruginosa and Staphylococcus aureus above 0.4 M. The magnitude of the effect of a particular ion is different between the two species suggesting a variety of mechanisms, including chao/kosmotropicity, may be operating (Lo Nostro et al 2006;Nostro et al 2005).…”

Section: Inhibition Of Processes By Chaotropicity and Kosmotropicitymentioning

confidence: 99%

The roles and applications of chaotropes and kosmotropes in industrial fermentation processes

Timson

2020

World J Microbiol Biotechnol

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Chaotropicity has long been recognised as a property of some compounds. Chaotropes tend to disrupt non-covalent interactions in biological macromolecules (e.g. proteins and nucleic acids) and supramolecular assemblies (e.g. phospholipid membranes). This results in the destabilisation and unfolding of these macromolecules and assemblies. Unsurprisingly, these compounds are typically harmful to living cells since they act against multiple targets, comprising cellular integrity and function. Kosmotropes are the opposite of chaotropes and these compounds promote the ordering and rigidification of biological macromolecules and assemblies. Since many biological macromolecules have optimum levels of flexibility, kosmotropes can also inhibit their activity and can be harmful to cells. Some products of industrial fermentations, most notably alcohols, are chaotropic. This property can be a limiting factor on rates of production and yields. It has been hypothesised that the addition of kosmotropes may mitigate the chaotropicity of some fermentation products. Some microbes naturally adapt to chaotropic environments by producing kosmotropic compatible solutes. Exploitation of this in industrial fermentations has been hampered by scientific and economic issues. The cost of the kosmotropes and their removal during purification needs to be considered. We lack a complete understanding of the chemistry of chaotropicity and a robust, quantitative framework for estimating overall chaotropicities of mixtures. This makes it difficult to predict the amount of kosmotrope required to neutralise the chaotropicity. This review considers examples of industrial fermentations where chaotropicity is an issue and suggests possible mitigations.

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Thermal Analysis on Bioprotectant Disaccharides by Elastic Incoherent Neutron Scattering

2013

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Stabilization effects of kosmotrope systems on ornithine carbamoyltransferase

Cited by 14 publications

References 49 publications

Molecular Basis of Interactions between the Antibiotic Nitrofurantoin and Human Serum Albumin: A Mechanism for the Rapid Drug Blood Transportation

Molecular Basis of Interactions between the Antibiotic Nitrofurantoin and Human Serum Albumin: A Mechanism for the Rapid Drug Blood Transportation

The roles and applications of chaotropes and kosmotropes in industrial fermentation processes

Thermal Analysis on Bioprotectant Disaccharides by Elastic Incoherent Neutron Scattering

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