Chromatography of carbon nanotubes separated albumin from other serum proteins: a method for direct analysis of their interactions

Y Kuboki, T Koshikawa, H Takita, R Fujisawa, MH Lee, S Abe, T Akasaka, M Uo, F Watari, Rachel Sammons

Research output: Contribution to journalArticle

14 Citations (Scopus)

Abstract

Chromatography technology was employed to clarify the mechanism of interaction between multi-wall carbon nanotubes (MWCNT) and proteins. A column (16x100 mm) was packed with purified MWCNT, and various proteins were eluted with phosphate buffered saline (PBS) with and without gradient systems. It was found that albumin in bovine serum was eluted immediately from the column without any adsorption to MWCNT. Conversely, the non-albumin proteins, including a protein of 85 kDa molecular mass and a group of proteins with molecular masses higher than 115 kDa, exhibited considerably high affinity towards MWCNT. A sample of pure bovine serum albumin was also eluted immediately from the column, while lysozyme did not elute as a peak with PBS, but eluted with 0.6 M NaCl. Fundamentally, carbon nanotubes are devoid of any electrical charge. Therefore, other forces including the hydrogen bonds, hydrophilic interactions, and van der Waals forces were most probably responsible for the differential elution behaviors. In conclusion, this chromatographic method provided a simple and direct analysis of the interactions between carbon nanotubes and the various proteins.
Original languageEnglish
Pages (from-to)369-373
Number of pages5
JournalDental Materials Journal
Volume29
Issue number4
Early online date2 Jul 2010
DOIs
Publication statusPublished - 2 Jul 2010

Fingerprint

Dive into the research topics of 'Chromatography of carbon nanotubes separated albumin from other serum proteins: a method for direct analysis of their interactions'. Together they form a unique fingerprint.

Cite this