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Chemical modification of Nitzschia panduriformis's frustules for protein and viral nanoparticle adsorption

Authors :
Wu, Meng-Chuan
Coca, John Jaime Perez
Chang, Gary Ro-Lin
Suen, Shing-Yi
Lin, Chia-Feng
Chou, Hong-Nong
Lai, Su-Yuan
Wang, Min-Ying
Source :
Process Biochemistry. Dec2012, Vol. 47 Issue 12, p2204-2210. 7p.
Publication Year :
2012

Abstract

Abstract: The frustule of diatoms, through appropriate chemical modification, can be developed for a high adsorption level of recombinant proteins and viral nanoparticles. Field emission scanning electron microscopy (FE-SEM) analysis of clean frustules revealed a 3D loculate areolae structure (valvar phase porous pattern of the siliceous cell wall). Isocyanatopropyl triethoxysilane (IPS) and iminodiacetic acid (IDA) were used to immobilize Cu2+ ions (an average Cu2+ adsorption capacity about 190μmol of Cu2+/ml of the Cu2+-coupled biosilica reached). FE-SEM, energy dispersion X-ray spectroscopy (EDS) and Fourier transform infrared (FT-IR) were used to confirm the chemical modification of the Cu2+-coupled biosilica. Protein adsorption was confirmed with the detection of a recombinant (His)6-tagged green fluorescent protein binding using fluorescent microscopy. Infectious bursal disease virus VP2-441 subviral particles (SVPs) were found to bind to the Cu2+-coupled biosilica (approximately 3×10−9 mol of VP2-441 SVPs/ml of modified frustules), a level higher than the previously obtained 9×10−10 mol/ml for SVP binding using a commercial Ni–NTA resin. These give diatom frustules the potential to be developed into a material useful in viral nanoparticle purification systems or as a biosensor for the detection of viruses. [Copyright &y& Elsevier]

Details

Language :
English
ISSN :
13595113
Volume :
47
Issue :
12
Database :
Academic Search Index
Journal :
Process Biochemistry
Publication Type :
Academic Journal
Accession number :
84162000
Full Text :
https://doi.org/10.1016/j.procbio.2012.08.015