Protein corona – from molecular adsorption to physiological complexity
In biological environments, nanoparticles are enshrouded by a layer of biomolecules, predominantly proteins, mediating its subsequent interactions with cells. Detecting this protein corona, understanding its formation with regards to nanoparticle (NP) and protein properties, and elucidating its biol...
| Main Authors: | , , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
Beilstein-Institut
2015-03-01
|
| Series: | Beilstein Journal of Nanotechnology |
| Subjects: | |
| Online Access: | https://doi.org/10.3762/bjnano.6.88 |
| _version_ | 1818540864019890176 |
|---|---|
| author | Lennart Treuel Dominic Docter Michael Maskos Roland H. Stauber |
| author_facet | Lennart Treuel Dominic Docter Michael Maskos Roland H. Stauber |
| author_sort | Lennart Treuel |
| collection | DOAJ |
| description | In biological environments, nanoparticles are enshrouded by a layer of biomolecules, predominantly proteins, mediating its subsequent interactions with cells. Detecting this protein corona, understanding its formation with regards to nanoparticle (NP) and protein properties, and elucidating its biological implications were central aims of bio-related nano-research throughout the past years. Here, we discuss the mechanistic parameters that are involved in the protein corona formation and the consequences of this corona formation for both, the particle, and the protein. We review consequences of corona formation for colloidal stability and discuss the role of functional groups and NP surface functionalities in shaping NP–protein interactions. We also elaborate the recent advances demonstrating the strong involvement of Coulomb-type interactions between NPs and charged patches on the protein surface. Moreover, we discuss novel aspects related to the complexity of the protein corona forming under physiological conditions in full serum. Specifically, we address the relation between particle size and corona composition and the latest findings that help to shed light on temporal evolution of the full serum corona for the first time. Finally, we discuss the most recent advances regarding the molecular-scale mechanistic role of the protein corona in cellular uptake of NPs. |
| first_indexed | 2024-12-11T22:00:58Z |
| format | Article |
| id | doaj.art-b58acd3d921e442dad30686ddf874609 |
| institution | Directory Open Access Journal |
| issn | 2190-4286 |
| language | English |
| last_indexed | 2024-12-11T22:00:58Z |
| publishDate | 2015-03-01 |
| publisher | Beilstein-Institut |
| record_format | Article |
| series | Beilstein Journal of Nanotechnology |
| spelling | doaj.art-b58acd3d921e442dad30686ddf8746092022-12-22T00:49:06ZengBeilstein-InstitutBeilstein Journal of Nanotechnology2190-42862015-03-016185787310.3762/bjnano.6.882190-4286-6-88Protein corona – from molecular adsorption to physiological complexityLennart Treuel0Dominic Docter1Michael Maskos2Roland H. Stauber3Fraunhofer ICT-IMM, Carl-Zeiss-Str. 18-20, 55219 Mainz, GermanyMolecular and Cellular Oncology/Mainz Screening Center (MSC), University Hospital of Mainz, Langenbeckstrasse 1, 55101 Mainz, GermanyFraunhofer ICT-IMM, Carl-Zeiss-Str. 18-20, 55219 Mainz, GermanyMolecular and Cellular Oncology/Mainz Screening Center (MSC), University Hospital of Mainz, Langenbeckstrasse 1, 55101 Mainz, GermanyIn biological environments, nanoparticles are enshrouded by a layer of biomolecules, predominantly proteins, mediating its subsequent interactions with cells. Detecting this protein corona, understanding its formation with regards to nanoparticle (NP) and protein properties, and elucidating its biological implications were central aims of bio-related nano-research throughout the past years. Here, we discuss the mechanistic parameters that are involved in the protein corona formation and the consequences of this corona formation for both, the particle, and the protein. We review consequences of corona formation for colloidal stability and discuss the role of functional groups and NP surface functionalities in shaping NP–protein interactions. We also elaborate the recent advances demonstrating the strong involvement of Coulomb-type interactions between NPs and charged patches on the protein surface. Moreover, we discuss novel aspects related to the complexity of the protein corona forming under physiological conditions in full serum. Specifically, we address the relation between particle size and corona composition and the latest findings that help to shed light on temporal evolution of the full serum corona for the first time. Finally, we discuss the most recent advances regarding the molecular-scale mechanistic role of the protein corona in cellular uptake of NPs.https://doi.org/10.3762/bjnano.6.88agglomerationcorona compositiondynamicsnanoparticlesprotein corona |
| spellingShingle | Lennart Treuel Dominic Docter Michael Maskos Roland H. Stauber Protein corona – from molecular adsorption to physiological complexity Beilstein Journal of Nanotechnology agglomeration corona composition dynamics nanoparticles protein corona |
| title | Protein corona – from molecular adsorption to physiological complexity |
| title_full | Protein corona – from molecular adsorption to physiological complexity |
| title_fullStr | Protein corona – from molecular adsorption to physiological complexity |
| title_full_unstemmed | Protein corona – from molecular adsorption to physiological complexity |
| title_short | Protein corona – from molecular adsorption to physiological complexity |
| title_sort | protein corona from molecular adsorption to physiological complexity |
| topic | agglomeration corona composition dynamics nanoparticles protein corona |
| url | https://doi.org/10.3762/bjnano.6.88 |
| work_keys_str_mv | AT lennarttreuel proteincoronafrommolecularadsorptiontophysiologicalcomplexity AT dominicdocter proteincoronafrommolecularadsorptiontophysiologicalcomplexity AT michaelmaskos proteincoronafrommolecularadsorptiontophysiologicalcomplexity AT rolandhstauber proteincoronafrommolecularadsorptiontophysiologicalcomplexity |