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Conformational changes of fibrinogen in dispersed carbon nanotubes

Authors Park , Khang D 

Received 8 May 2012

Accepted for publication 15 June 2012

Published 6 August 2012 Volume 2012:7 Pages 4325—4333


Checked for plagiarism Yes

Review by Single anonymous peer review

Peer reviewer comments 5

Sung Jean Park,1 Dongwoo Khang2

1College of Pharmacy, Gachon University, Yeonsu-gu, Incheon, South Korea; 2School of Nano and Advanced Materials Science Engineering and Center for PRC and RIGET, Gyeongsang National University, Jinju, South Korea

Abstract: The conformational changes of plasma protein structures in response to carbon nanotubes are critical for determining the nanotoxicity and blood coagulation effects of carbon nanotubes. In this study, we identified that the functional intensity of carboxyl groups on carbon nanotubes, which correspond to the water dispersity or hydrophilicity of carbon nanotubes, can induce conformational changes in the fibrinogen domains. Also, elevation of carbon nanotube density can alter the secondary structures (ie, helices and beta sheets) of fibrinogen. Furthermore, fibrinogen that had been in contact with the nanoparticle material demonstrated a different pattern of heat denaturation compared with free fibrinogen as a result of a variation in hydrophilicity and concentration of carbon nanotubes. Considering the importance of interactions between carbon nanotubes and plasma proteins in the drug delivery system, this study elucidated the correlation between nanoscale physiochemical material properties of carbon nanotubes and associated structural changes in fibrinogen.

Keywords: carbon nanotubes, fibrinogen, nanotoxicity, conformational change, denaturation

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