Please use this identifier to cite or link to this item: https://doi.org/10.1016/j.biomaterials.2008.10.037
Title: Imaging the disruption of phospholipid monolayer by protein-coated nanoparticles using ordering transitions of liquid crystals
Authors: Hartono, D. 
Qin, W.J. 
Yang, K.-L. 
Yung, L.-Y.L. 
Keywords: Gold nanoparticles
Hydrophobic interactions
Liquid crystals
Phospholipids
Proteins
Issue Date: Feb-2009
Citation: Hartono, D., Qin, W.J., Yang, K.-L., Yung, L.-Y.L. (2009-02). Imaging the disruption of phospholipid monolayer by protein-coated nanoparticles using ordering transitions of liquid crystals. Biomaterials 30 (5) : 843-849. ScholarBank@NUS Repository. https://doi.org/10.1016/j.biomaterials.2008.10.037
Abstract: We report an easily visualized liquid crystal (LC)-based system to study the molecular interactions between protein-coated gold nanoparticles (AuNPs) and supported phospholipid monolayer self-assembled at the aqueous-LC interface. Protein-coated AuNPs were found to disrupt the phospholipid monolayer and resulted in the orientational transitions of LCs that support the phospholipid layer. The disruption of the phospholipid monolayer depends on the type of protein (albumin, neutravidin, and fibrinogen) adsorbing onto nanoparticles. Furthermore, our results suggest that hydrophobic interaction plays a major role in the disruption of the phospholipid layer by protein-coated AuNPs. Results obtained from this study may offer new understanding in the potential cytotoxicity of nanomaterials, where the interaction between nanoparticles and cell membrane is an important step. © 2008 Elsevier Ltd. All rights reserved.
Source Title: Biomaterials
URI: http://scholarbank.nus.edu.sg/handle/10635/64055
ISSN: 01429612
DOI: 10.1016/j.biomaterials.2008.10.037
Appears in Collections:Staff Publications

Show full item record
Files in This Item:
There are no files associated with this item.

Google ScholarTM

Check

Altmetric


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.