Biocompatibility of mannan nanogel-safe interaction with plasma proteins
(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)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/2883816
- author
- 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
- organization
- publishing date
- 2012
- 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
- pmid:22554917
- 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
- 2016-04-01 13:35:51
- date last changed
- 2023-10-01 04:01:01
@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}},
keywords = {{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}},
doi = {{10.1016/j.bbagen.2012.04.015}},
volume = {{1820}},
year = {{2012}},
}