КФУ. Карточка публикации. Binding of L-tryptophan and bovine serum albumin by novel goldnanoparticles capped with amphiphilicsulfonatomethylated calixresorcinarenes

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BINDING OF L-TRYPTOPHAN AND BOVINE SERUM ALBUMIN BY NOVEL GOLDNANOPARTICLES CAPPED WITH AMPHIPHILICSULFONATOMETHYLATED CALIXRESORCINARENES

Форма представления

Статьи в зарубежных журналах и сборниках

Год публикации

2019

Язык

английский

Авторы, сотрудники КФУ

Антипин Игорь Сергеевич, автор

Морозова Юлия Эрнестовна, автор

Шалаева Яна Викторовна, автор

Другие авторы

Кадиров Марсил Кахирович, автор

Низамеев Ирек Рашатович, автор

Авторы, аспиранты КФУ

Шуматбаева Алина Марселовна, автор

Библиографическое описание на языке оригинала

Ya.V.Shalaeva, Binding of L-tryptophan and bovine serum albumin by novel goldnanoparticles capped with amphiphilicsulfonatomethylated calixresorcinarenes / Ya.V.Shalaeva, Ju.E.Morozova, A.M.Shumatbaeva, I.R.Nizameev, M.K.Kadirov, I.S.Antipin // Journal of Molecular Liquids - 2019. – V. 286, 110879. DOI: 10.1016/j.molliq.2019.110879

Аннотация

A simple, one-step synthesis of spherical gold nanoparticles (d core = 38 and 25 nm) in aqueous solution has been carried out using sulfonatomethylated calixresorcinarenes with methyl (C1S) and pentyl (C5S) substituents on the lower rim both as reducing and stabilizing agents. The nanoparticles obtained, Au@C1S and Au@C5S, were characterized by absorption spectrophotometry, TEM, DLS, IR and TGA. The gold nanoparticles are stabilized by the interaction that occurs between macrocycles' sulfo-groups and the metal surface. It has been shown, that Au@C5S nanoparticles have a higher thermal stability than Au@C1S nanoparticles due to the denser packing of the macrocycle on the surface of gold nanoparticles caused by amphiphilic nature of the C5S macrocycle. C5S or Au@C5S associate cooperatively with L-tryptophan to form a nanoscale system capable of a spectral response to changing pH in aqueous solution. A detailed study of the interaction of С5S and Au@C5S with BSA in aqueous solution was carried out by spectro- photometry, DLS and ﬂuorimetry. It was found that C5S and Au@C5S both form stable complexes with the protein, which was conﬁrmed by the static character of the quenching of BSA ﬂuorescence. The mechanism of the interaction of BSA with the macrocycles in aqueous solution and on the surface of gold nanoparticles was investigated. The quenching (K SV ) and binding (K as ) constants, the number of binding sites (n), and thermodynamic interaction parameters (ΔG, ΔH, ΔS) were calculated. It was found that the process of protein binding by the free macrocycle and the modiﬁed gold nanoparticles is exothermic and spontaneous, and hydrogen bonding and van der Waals interactions make a major contribution into the binding. The synchronous ﬂuorescence method showed that the binding of BSA with macrocycle inﬂuences the microenvironment of the tryptophan residues in protein molecule. The interaction of С5S and Au@C5S with BSA leads to the changes in the protein structure as well as in the physicochemical characteristics of gold nanoparticles, which is a promising aspect in the use of such systems for transport of protein molecules or their visualization-detection in biological media.

Ключевые слова

Calixresorcinarene, Gold nanoparticle, L-Tryptophan, Bovine serum albumin, Fluorescence spectroscopy

Название журнала

Journal of Molecular Liquids

URL

https://www.sciencedirect.com/science/article/pii/S016773221836642X?via%3Dihub

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https://repository.kpfu.ru/?p_id=241491

Полная запись метаданных

Поле DC	Значение	Язык
dc.contributor.author	Антипин Игорь Сергеевич	ru_RU
dc.contributor.author	Морозова Юлия Эрнестовна	ru_RU
dc.contributor.author	Шалаева Яна Викторовна	ru_RU
dc.contributor.author	Кадиров Марсил Кахирович	ru_RU
dc.contributor.author	Низамеев Ирек Рашатович	ru_RU
dc.contributor.author	Шуматбаева Алина Марселовна	ru_RU
dc.date.accessioned	2019-01-01T00:00:00Z	ru_RU
dc.date.available	2019-01-01T00:00:00Z	ru_RU
dc.date.issued	2019	ru_RU
dc.identifier.citation	Ya.V.Shalaeva, Binding of L-tryptophan and bovine serum albumin by novel goldnanoparticles capped with amphiphilicsulfonatomethylated calixresorcinarenes / Ya.V.Shalaeva, Ju.E.Morozova, A.M.Shumatbaeva, I.R.Nizameev, M.K.Kadirov, I.S.Antipin // Journal of Molecular Liquids - 2019. – V. 286, 110879. DOI: 10.1016/j.molliq.2019.110879	ru_RU
dc.identifier.uri	https://repository.kpfu.ru/?p_id=241491	ru_RU
dc.description.abstract	Journal of Molecular Liquids	ru_RU
dc.description.abstract	A simple, one-step synthesis of spherical gold nanoparticles (d core = 38 and 25 nm) in aqueous solution has been carried out using sulfonatomethylated calixresorcinarenes with methyl (C1S) and pentyl (C5S) substituents on the lower rim both as reducing and stabilizing agents. The nanoparticles obtained, Au@C1S and Au@C5S, were characterized by absorption spectrophotometry, TEM, DLS, IR and TGA. The gold nanoparticles are stabilized by the interaction that occurs between macrocycles' sulfo-groups and the metal surface. It has been shown, that Au@C5S nanoparticles have a higher thermal stability than Au@C1S nanoparticles due to the denser packing of the macrocycle on the surface of gold nanoparticles caused by amphiphilic nature of the C5S macrocycle. C5S or Au@C5S associate cooperatively with L-tryptophan to form a nanoscale system capable of a spectral response to changing pH in aqueous solution. A detailed study of the interaction of С5S and Au@C5S with BSA in aqueous solution was carried out by spectro- photometry, DLS and ﬂuorimetry. It was found that C5S and Au@C5S both form stable complexes with the protein, which was conﬁrmed by the static character of the quenching of BSA ﬂuorescence. The mechanism of the interaction of BSA with the macrocycles in aqueous solution and on the surface of gold nanoparticles was investigated. The quenching (K SV ) and binding (K as ) constants, the number of binding sites (n), and thermodynamic interaction parameters (ΔG, ΔH, ΔS) were calculated. It was found that the process of protein binding by the free macrocycle and the modiﬁed gold nanoparticles is exothermic and spontaneous, and hydrogen bonding and van der Waals interactions make a major contribution into the binding. The synchronous ﬂuorescence method showed that the binding of BSA with macrocycle inﬂuences the microenvironment of the tryptophan residues in protein molecule. The interaction of С5S and Au@C5S with BSA leads to the changes in the protein structure as well as in the physicochemical characteristics of gold nanoparticles, which is a promising aspect in the use of such systems for transport of protein molecules or their visualization-detection in biological media.	ru_RU
dc.language.iso	ru	ru_RU
dc.subject	Calixresorcinarene	ru_RU
dc.subject	Gold nanoparticle	ru_RU
dc.subject	L-Tryptophan	ru_RU
dc.subject	Bovine serum albumin	ru_RU
dc.subject	Fluorescence spectroscopy	ru_RU
dc.title	Binding of L-tryptophan and bovine serum albumin by novel goldnanoparticles capped with amphiphilicsulfonatomethylated calixresorcinarenes	ru_RU
dc.type	Статьи в зарубежных журналах и сборниках	ru_RU