期刊
JOURNAL OF COLLOID AND INTERFACE SCIENCE
卷 587, 期 -, 页码 150-161出版社
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.jcis.2020.12.025
关键词
Gold nanoparticles; Cytochrome c; Orientation; Apoptosis; Peroxidase activity
资金
- Engineering and Physical Sciences Research Council (EPSRC) [EP/R004072/1]
- EU ERDF (FEDER)
- Spanish government [TEC2017-85059-C3-2-R]
- University of Nottingham
- EPSRC [EP/M005178/1]
- EPSRC [EP/R004072/1, EP/P031684/1] Funding Source: UKRI
Protein orientation on the surface of nanoparticles plays a crucial role in modulating their biological activity, and can be altered by changing the adsorption orientation. This has important implications for the design of new nanoscale biosensors and nanomedicines.
Protein orientation in nanoparticle-protein conjugates plays a crucial role in binding to cell receptors and ultimately, defines their targeting efficiency. Therefore, understanding fundamental aspects of the role of protein orientation upon adsorption on the surface of nanoparticles (NPs) is vital for the development of clinically important protein-based nanomedicines. In this work, new insights on the effect of the different orientation of cytochrome c (cyt c) bound to gold nanoparticles (GNPs) using various ligands on its apoptotic activity is reported. Time-of-Flight Secondary-Ion Mass Spectrometry (ToF-SIMS), electrochemical and circular dichroism (CD) analyses are used to investigate the characteristics of cyt c orientation and structure on functionalized GNPs. These studies indicate that the orientation and position of the heme ring inside the cyt c structure can be altered by changing the surface chemistry on the GNPs. A difference in the apoptosis inducing capability because of different orientation of cyt c bound to the GNPs is observed. These findings indicate that the biological activity of a protein can be modulated on the surface of NPs by varying its adsorption orientation. This study will impact on the rational design of new nanoscale biosensors, bioelectronics, and nanoparticle-protein based drugs. (c) 2020 Elsevier Inc. All rights reserved.
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