liu.seSearch for publications in DiVA
Change search
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • harvard1
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • oxford
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf
Protein particles formed by protein activation and spontaneous self-assembly
Hong Kong University of Science and Technology, Clear Water Bay, Hong Kong, China.ORCID iD: 0000-0003-3274-6029
Berlin-Brandenburg Center of Regenerative Therapies, Charité-Universitätsmedizin Berlin, Germany.
Hong Kong University of Science and Technology, Clear Water Bay, Hong Kong, China.
Berlin-Brandenburg Center of Regenerative Therapies, Charité-Universitätsmedizin Berlin, Germany.
2010 (English)In: Advanced Functional Materials, ISSN 1616-301X, E-ISSN 1616-3028, Vol. 20, no 23, 4139-4144 p.Article in journal (Refereed) Published
Abstract [en]

In this article, a non-chemical crosslinking method is used to produce pure protein microparticles with an innovative approach, so-called protein activation spontaneous and self-assembly (PASS). The fabrication of protein microparticles is based on the idea of using the internal disulfide bridges within protein molecules as molecular linkers to assemble protein molecules into a microparticle form. The assembly process is triggered by an activating reagent–dithiothreitol (DTT), which only involved in the intermediate step without being incorporated into the resulting protein microparticles. Conventional protein microparticle fabrication methods usually involve emulsification process and chemical crosslink reactions using amine reactive reagents such as glutaraldehdye or EDC/NHS. The resulting protein microparticles are usually having various size distributions. Most importantly crosslinking reactions using amine reactive reagents will result in producing protein microparticles with undesired properties such as auto-fluorescence and high toxicity. In contrast to the conventional methods, our technology provides a simple and robust method to produce highly homogeneous, stable and non-fluorescence pure protein microparticles under mild conditions at physiological pH and temperature. The protein microparticles are found to be biodegradable, non-toxic to MDCK cells and with preserved biological activities. Results on the cytotoxcity study and enzyme function demonstrate the potential applications of the protein microparticles in the area of pharmaceutics and analytical chemistry.

Place, publisher, year, edition, pages
John Wiley & Sons, 2010. Vol. 20, no 23, 4139-4144 p.
Keyword [en]
protein; self-assembly; cysteine; dithiothreitol; particles
National Category
Medical Materials
Identifiers
URN: urn:nbn:se:liu:diva-92050DOI: 10.1002/adfm.201001205OAI: oai:DiVA.org:liu-92050DiVA: diva2:620031
Available from: 2013-05-07 Created: 2013-05-07 Last updated: 2017-12-06Bibliographically approved

Open Access in DiVA

No full text

Other links

Publisher's full text

Authority records BETA

Mak, Wing Cheung

Search in DiVA

By author/editor
Mak, Wing Cheung
In the same journal
Advanced Functional Materials
Medical Materials

Search outside of DiVA

GoogleGoogle Scholar

doi
urn-nbn

Altmetric score

doi
urn-nbn
Total: 211 hits
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • harvard1
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • oxford
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf