Protein-Nanoparticle Interactions: Opportunities and Challenges

被引:1161
作者
Mahmoudi, Morteza [1 ,2 ]
Lynch, Iseult [3 ,4 ]
Ejtehadi, Mohammad Reza [5 ]
Monopoli, Marco P. [3 ,4 ]
Bombelli, Francesca Baldelli [6 ]
Laurent, Sophie [7 ]
机构
[1] Pasteur Inst Iran, Natl Cell Bank, Tehran, Iran
[2] Univ Tehran Med Sci, Fac Pharm, Nanotechnol Res Ctr, Tehran, Iran
[3] Univ Coll Dublin, Sch Chem & Chem Biol, Dublin 4, Ireland
[4] Univ Coll Dublin, Conway Inst Biomol & Biomed Res, Dublin 4, Ireland
[5] Sharif Univ Technol, Dept Phys, Tehran, Iran
[6] UEA, Sch Pharm, Norwich, Norfolk, England
[7] Univ Mons, NMR & Mol Imaging Lab, Dept Gen Organ & Biomed Chem, B-7000 Mons, Belgium
关键词
BOVINE SERUM-ALBUMIN; IRON-OXIDE NANOPARTICLES; WALLED CARBON NANOTUBES; MOLECULAR-DYNAMICS SIMULATIONS; INDUCED CONFORMATIONAL-CHANGES; QUARTZ-CRYSTAL MICROBALANCE; COATED GOLD NANOPARTICLES; RESONANCE ENERGY-TRANSFER; QUANTUM-DOT FLUORESCENCE; CYTOCHROME-C;
D O I
10.1021/cr100440g
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
The significant role of protein nanoparticle interactions in nanomedicine and nanotoxicity is emerging recently through the identification of the nanoparticles (NP) protein (biomolecule) corona. The dynamic layer of proteins and/or other biomolecules adsorbed to the nanoparticle surface determines how a NP interacts with living systems and thereby modifies the cellular responses to the NP. Ehrenberg and co-workers used cultured endothelium cells as a model for vascular transport of polystyrene NP with various functional groups, which showed that the capacity of the various NP surfaces to adsorb proteins was indicative of their tendency to associate with cells. The quantification of the adsorbed proteins showed that high-binding NP were maximally coated within seconds to minutes, indicating that proteins on the surface of NP could mediate cell association over much longer time scales. The adsorption or covalent binding of a protein onto a NP's surface can strongly alter the physio-chemical and structural properties of both of them.
引用
收藏
页码:5610 / 5637
页数:28
相关论文
共 249 条
[1]   Nanoparticle interaction with plasma proteins as it relates to particle biodistribution, biocompatibility and therapeutic efficacy [J].
Aggarwal, Parag ;
Hall, Jennifer B. ;
McLeland, Christopher B. ;
Dobrovolskaia, Marina A. ;
McNeil, Scott E. .
ADVANCED DRUG DELIVERY REVIEWS, 2009, 61 (06) :428-437
[2]  
AISEN P, 1973, INORG CHEM, pCH9
[3]   Manufacture and use of nanomaterials: current status in the UK and global trends [J].
Aitken, R. J. ;
Chaudhry, M. Q. ;
Boxall, A. B. A. ;
Hull, M. .
OCCUPATIONAL MEDICINE-OXFORD, 2006, 56 (05) :300-306
[4]   Semiconductor clusters, nanocrystals, and quantum dots [J].
Alivisatos, AP .
SCIENCE, 1996, 271 (5251) :933-937
[5]   Mechanism of water permeation through modified carbon nanotubes as a model for peptide nanotube channels [J].
Alizadeh, Ali ;
Parsafar, Golam Abbas ;
Ejtehadi, Mohammad Reza .
INTERNATIONAL JOURNAL OF NANOTECHNOLOGY, 2009, 6 (10-11) :926-941
[6]  
Allemann E, 1997, J BIOMED MATER RES, V37, P229, DOI 10.1002/(SICI)1097-4636(199711)37:2<229::AID-JBM12>3.0.CO
[7]  
2-9
[8]   STRUCTURE OF HUMAN LACTOFERRIN AT 3.2-A RESOLUTION [J].
ANDERSON, BF ;
BAKER, HM ;
DODSON, EJ ;
NORRIS, GE ;
RUMBALL, SV ;
WATERS, JM ;
BAKER, EN .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1987, 84 (07) :1769-1773
[9]   STRUCTURE OF HUMAN LACTOFERRIN - CRYSTALLOGRAPHIC STRUCTURE-ANALYSIS AND REFINEMENT AT 2.8-A RESOLUTION [J].
ANDERSON, BF ;
BAKER, HM ;
NORRIS, GE ;
RICE, DW ;
BAKER, EN .
JOURNAL OF MOLECULAR BIOLOGY, 1989, 209 (04) :711-734
[10]   Biological responses to materials [J].
Anderson, JM .
ANNUAL REVIEW OF MATERIALS RESEARCH, 2001, 31 :81-110