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Biocompatibility of mannan nanogel-safe interaction with plasma proteins

Ferreira, Silvia A.; Oslakovic, Cecilia LU ; Cukalevski, Risto LU ; Frohm, Birgitta LU ; Dahlbäck, Björn LU ; Linse, Sara LU ; Gama, Francisco M. and Cedervall, Tommy LU (2012) In Biochimica et Biophysica Acta. General Subjects 1820(7). p.1043-1051
Abstract
Background: Self-assembled mannan nanogels are designed to provide a therapeutic or vaccine delivery platform based on the bioactive properties of mannan to target mannose receptor expressed on the surface of antigen-presenting cells, combined with the performance of nanogels as carriers of biologically active agents. Methods: Proteins in the corona around mannan nanogel formed in human plasma were identified by mass spectrometry after size exclusion chromatography or centrifugation followed by sodium dodecyl sulfate polyacrylamide gel electrophoresis. Structural changes and time dependent binding of human apolipoprotein A-I (apoA-I) and human serum albumin (HSA) to mannan nanogel were studied using intrinsic tryptophan fluorescence and... (More)
Background: Self-assembled mannan nanogels are designed to provide a therapeutic or vaccine delivery platform based on the bioactive properties of mannan to target mannose receptor expressed on the surface of antigen-presenting cells, combined with the performance of nanogels as carriers of biologically active agents. Methods: Proteins in the corona around mannan nanogel formed in human plasma were identified by mass spectrometry after size exclusion chromatography or centrifugation followed by sodium dodecyl sulfate polyacrylamide gel electrophoresis. Structural changes and time dependent binding of human apolipoprotein A-I (apoA-I) and human serum albumin (HSA) to mannan nanogel were studied using intrinsic tryptophan fluorescence and circular dichroism spectroscopy. The mannan nanogel effect on blood coagulation and fibrillation of Alzheimer's disease-associated amyloid beta peptide and hemodialysis-associated amyloidosis beta 2 microglobulin was evaluated using thrombin generation assay or thioflavin T fluorescence assay, respectively. Results: The protein corona around mannan nanogel is formed through a slow process, is quite specific comprising apolipoproteins B-100, A-I and E and HSA, evolves over time, and the equilibrium is reached after hours to days. Structural changes and time dependent binding of apoA-I and HSA to mannan nanogel are minor. The mannan nanogel does not affect blood coagulation and retards the fibril formation. Conclusions: Mannan nanogel has a high biosafety and biocompatibility, which is mandatory for nanomaterials to be used in biomedical applications. General Significance: Our research provides a molecular approach to evaluate the safety aspects of nanomaterials, which is of general concern in society and science. (C) 2012 Elsevier B.V. All rights reserved. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
Mannan nanogel, Protein corona, Coagulation, Fibrillation, Biosafety, Biocompatibility
in
Biochimica et Biophysica Acta. General Subjects
volume
1820
issue
7
pages
1043 - 1051
publisher
Elsevier
external identifiers
  • wos:000305366100031
  • scopus:84860821259
ISSN
0304-4165
DOI
10.1016/j.bbagen.2012.04.015
language
English
LU publication?
yes
id
12ea68e6-bf55-4177-9467-c46e3a6a6ce0 (old id 2883816)
date added to LUP
2012-08-01 09:42:02
date last changed
2017-07-23 04:09:19
@article{12ea68e6-bf55-4177-9467-c46e3a6a6ce0,
  abstract     = {Background: Self-assembled mannan nanogels are designed to provide a therapeutic or vaccine delivery platform based on the bioactive properties of mannan to target mannose receptor expressed on the surface of antigen-presenting cells, combined with the performance of nanogels as carriers of biologically active agents. Methods: Proteins in the corona around mannan nanogel formed in human plasma were identified by mass spectrometry after size exclusion chromatography or centrifugation followed by sodium dodecyl sulfate polyacrylamide gel electrophoresis. Structural changes and time dependent binding of human apolipoprotein A-I (apoA-I) and human serum albumin (HSA) to mannan nanogel were studied using intrinsic tryptophan fluorescence and circular dichroism spectroscopy. The mannan nanogel effect on blood coagulation and fibrillation of Alzheimer's disease-associated amyloid beta peptide and hemodialysis-associated amyloidosis beta 2 microglobulin was evaluated using thrombin generation assay or thioflavin T fluorescence assay, respectively. Results: The protein corona around mannan nanogel is formed through a slow process, is quite specific comprising apolipoproteins B-100, A-I and E and HSA, evolves over time, and the equilibrium is reached after hours to days. Structural changes and time dependent binding of apoA-I and HSA to mannan nanogel are minor. The mannan nanogel does not affect blood coagulation and retards the fibril formation. Conclusions: Mannan nanogel has a high biosafety and biocompatibility, which is mandatory for nanomaterials to be used in biomedical applications. General Significance: Our research provides a molecular approach to evaluate the safety aspects of nanomaterials, which is of general concern in society and science. (C) 2012 Elsevier B.V. All rights reserved.},
  author       = {Ferreira, Silvia A. and Oslakovic, Cecilia and Cukalevski, Risto and Frohm, Birgitta and Dahlbäck, Björn and Linse, Sara and Gama, Francisco M. and Cedervall, Tommy},
  issn         = {0304-4165},
  keyword      = {Mannan nanogel,Protein corona,Coagulation,Fibrillation,Biosafety,Biocompatibility},
  language     = {eng},
  number       = {7},
  pages        = {1043--1051},
  publisher    = {Elsevier},
  series       = {Biochimica et Biophysica Acta. General Subjects},
  title        = {Biocompatibility of mannan nanogel-safe interaction with plasma proteins},
  url          = {http://dx.doi.org/10.1016/j.bbagen.2012.04.015},
  volume       = {1820},
  year         = {2012},
}