Document Detail


Nanoparticle surface charge mediates the cellular receptors used by protein-nanoparticle complexes.
MedLine Citation:
PMID:  22774860     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Nanoparticles are increasingly important for biological applications ranging from drug delivery to cellular imaging. In the course of these applications, nanoparticles are exposed to a complex environment of extracellular proteins that can be adsorbed onto the surface of the nanoparticle, altering nanoparticle-cell interactions. We have investigated how proteins found in blood serum affect the binding of nanoparticles to the surface of cells. Using fluorescence microscopy, we find that the cellular binding of cationic nanoparticles is enhanced by the presence of serum proteins, while the binding of anionic nanoparticles is inhibited. We have determined that this difference in cellular binding is due to the use of distinct cellular receptors. Competition assays, quantified with flow cytometry, show that the protein-nanoparticle complex formed from the cationic nanoparticles binds to scavenger receptors on the cell surface. Interestingly, the protein-nanoparticle complex formed from anionic nanoparticles binds to native protein receptors. As nanoparticles become increasingly important for in vivo applications, we expect these results will inform the design of nanoparticles with improved cellular binding.
Authors:
Candace C Fleischer; Christine K Payne
Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, U.S. Gov't, Non-P.H.S.     Date:  2012-07-20
Journal Detail:
Title:  The journal of physical chemistry. B     Volume:  116     ISSN:  1520-5207     ISO Abbreviation:  J Phys Chem B     Publication Date:  2012 Aug 
Date Detail:
Created Date:  2012-08-02     Completed Date:  2012-12-03     Revised Date:  2013-08-12    
Medline Journal Info:
Nlm Unique ID:  101157530     Medline TA:  J Phys Chem B     Country:  United States    
Other Details:
Languages:  eng     Pagination:  8901-7     Citation Subset:  IM    
Affiliation:
School of Chemistry and Biochemistry and Petit Institute for Bioengineering and Bioscience, Georgia Institute of Technology, 901 Atlantic Drive, Atlanta, Georgia 30332, USA.
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MeSH Terms
Descriptor/Qualifier:
Animals
Anions / chemistry
Cations / chemistry
Cell Line
Cercopithecus aethiops
Nanoparticles / chemistry*
Polystyrenes / chemistry
Protein Binding
Proteins / chemistry*,  metabolism
Surface Properties
Grant Support
ID/Acronym/Agency:
1DP2OD006470/OD/NIH HHS; DP2 OD006470/OD/NIH HHS
Chemical
Reg. No./Substance:
0/Anions; 0/Cations; 0/Polystyrenes; 0/Proteins
Comments/Corrections

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