Cytochrome c conjugated to ZnO-MAA nanoparticles: the study of interaction and influence on protein structure
Jazyk angličtina Země Nizozemsko Médium print-electronic
Typ dokumentu časopisecké články, práce podpořená grantem
PubMed
23628581
DOI
10.1016/j.ijbiomac.2013.04.064
PII: S0141-8130(13)00247-X
Knihovny.cz E-zdroje
- MeSH
- adsorpce MeSH
- cirkulární dichroismus MeSH
- cytochromy c chemie MeSH
- imobilizované proteiny chemie MeSH
- koncentrace vodíkových iontů MeSH
- koně MeSH
- mikroskopie atomárních sil MeSH
- myokard chemie MeSH
- nanočástice chemie ultrastruktura MeSH
- oxid zinečnatý chemie MeSH
- spektrofotometrie MeSH
- thioglykoláty chemie MeSH
- velikost částic MeSH
- zvířata MeSH
- Check Tag
- zvířata MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Názvy látek
- 2-mercaptoacetate MeSH Prohlížeč
- cytochromy c MeSH
- imobilizované proteiny MeSH
- oxid zinečnatý MeSH
- thioglykoláty MeSH
Nanoparticle-protein conjugates have potential for numerous applications due to the combination of the properties of both components. In this paper we studied the conjugation of horse heart cytochrome c with ZnO nanoparticles modified by mercaptoacetic acid (MAA) which may be a material with great potential in anticancer therapy as a consequence of synergic effect of both components. Cyt c adsorption to the ZnO-MAA NPs surface was studied by UV-vis spectroscopy and by a dynamic light scattering in various pH. The results indicate that the optimal pH for the association of protein with modified nanoparticles is in range 5.8-8.5 where 90-96% of cytochrome c was assembled on ZnO-MAA nanoparticles. The interaction of proteins with nanoparticles often results in denaturation or loss of protein function. Our observations from UV-vis spectroscopy and circular dichroism performed preserved protein structure after the interaction with modified nanoparticles.
Citace poskytuje Crossref.org