KFU. Card publication. 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

Form of presentation

Articles in international journals and collections

Year of publication

2019

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Authors, employees of KFU

Antipin Igor Sergeevich, author

Morozova Yuliya Ernestovna, author

Shalaeva Yana Viktorovna, author

Other authors

Kadirov Marsil Kakhirovich, author

Nizameev Irek Rashatovich, author

Authors, postgraduates KFU

Shumatbaeva Alina Marselovna, postgraduate kfu

Bibliographic description in the original language

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

Annotation

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 �5S 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 �5S 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.

Keywords

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

The name of the journal

Journal of Molecular Liquids

URL

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

Please use this ID to quote from or refer to the card

https://repository.kpfu.ru/eng/?p_id=241491&p_lang=2

Full metadata record

Field DC	Value	Language
dc.contributor.author	Antipin Igor Sergeevich	ru_RU
dc.contributor.author	Morozova Yuliya Ernestovna	ru_RU
dc.contributor.author	Shalaeva Yana Viktorovna	ru_RU
dc.contributor.author	Kadirov Marsil Kakhirovich	ru_RU
dc.contributor.author	Nizameev Irek Rashatovich	ru_RU
dc.contributor.author	Shumatbaeva Alina Marselovna	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/eng/?p_id=241491&p_lang=2	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 �5S 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 �5S 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	Articles in international journals and collections	ru_RU