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Interaction of Human Serum Album and C(60) Aggregates in Solution

An important property of C(60) in aquatic ecotoxicology is that it can form stable aggregates with nanoscale dimensions, namely nC(60). Aggregation allows fullerenes to remain suspended for a long time, and the reactivity of individual C(60) is substantially altered in this aggregate form. Herein, w...

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Detalles Bibliográficos
Autores principales: Song, Maoyong, Liu, Shufang, Yin, Junfa, Wang, Hailin
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Molecular Diversity Preservation International (MDPI) 2011
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3179145/
https://www.ncbi.nlm.nih.gov/pubmed/21954338
http://dx.doi.org/10.3390/ijms12084964
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author Song, Maoyong
Liu, Shufang
Yin, Junfa
Wang, Hailin
author_facet Song, Maoyong
Liu, Shufang
Yin, Junfa
Wang, Hailin
author_sort Song, Maoyong
collection PubMed
description An important property of C(60) in aquatic ecotoxicology is that it can form stable aggregates with nanoscale dimensions, namely nC(60). Aggregation allows fullerenes to remain suspended for a long time, and the reactivity of individual C(60) is substantially altered in this aggregate form. Herein, we investigated the interaction of nC(60) and human serum album (HSA) using the methods of fluorescence, fluorescence dynamics, circular dichroism (CD), and site marker competitive experiments. We proposed a binding model consistent with the available experimental results for the interactions of nC(60) with HSA. During the interaction process, the structure and conformation of HSA were affected, leading to functional changes of drug binding sites of HSA.
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spelling pubmed-31791452011-09-27 Interaction of Human Serum Album and C(60) Aggregates in Solution Song, Maoyong Liu, Shufang Yin, Junfa Wang, Hailin Int J Mol Sci Article An important property of C(60) in aquatic ecotoxicology is that it can form stable aggregates with nanoscale dimensions, namely nC(60). Aggregation allows fullerenes to remain suspended for a long time, and the reactivity of individual C(60) is substantially altered in this aggregate form. Herein, we investigated the interaction of nC(60) and human serum album (HSA) using the methods of fluorescence, fluorescence dynamics, circular dichroism (CD), and site marker competitive experiments. We proposed a binding model consistent with the available experimental results for the interactions of nC(60) with HSA. During the interaction process, the structure and conformation of HSA were affected, leading to functional changes of drug binding sites of HSA. Molecular Diversity Preservation International (MDPI) 2011-08-04 /pmc/articles/PMC3179145/ /pubmed/21954338 http://dx.doi.org/10.3390/ijms12084964 Text en © 2011 by the authors; licensee MDPI, Basel, Switzerland. http://creativecommons.org/licenses/by/3.0 This article is an open-access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/3.0/).
spellingShingle Article
Song, Maoyong
Liu, Shufang
Yin, Junfa
Wang, Hailin
Interaction of Human Serum Album and C(60) Aggregates in Solution
title Interaction of Human Serum Album and C(60) Aggregates in Solution
title_full Interaction of Human Serum Album and C(60) Aggregates in Solution
title_fullStr Interaction of Human Serum Album and C(60) Aggregates in Solution
title_full_unstemmed Interaction of Human Serum Album and C(60) Aggregates in Solution
title_short Interaction of Human Serum Album and C(60) Aggregates in Solution
title_sort interaction of human serum album and c(60) aggregates in solution
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3179145/
https://www.ncbi.nlm.nih.gov/pubmed/21954338
http://dx.doi.org/10.3390/ijms12084964
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AT wanghailin interactionofhumanserumalbumandc60aggregatesinsolution