Structure and function of glucose binding protein-single walled carbon nanotube complexes.
Understanding the structure and function of glucose binding proteins (GBP) complexed with single walled carbon nanotubes (SWNTs) is important for the development of applications including fluorescent sensors and nanostructure particle tracking. Herein, circular dichroism (CD), thermal denaturation, photo-absorption spectroscopy and atomic force microscopy are used to study these nanostructures. The protein retains its glucose-binding activity after complexation and is thermally stable below 36 °C. However, the SWNT lowers the midpoint denaturation temperature (Tm) by 5 °C and 4 °C in the absence and presence of 10 mM glucose, respectively. This data highlights that using techniques such as CD and thermal denaturation may be necessary to fully characterize such protein-nanomaterial nanostructures.
Department of Chemical Engineering, The Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, United States.
Thomas P
TP
McNicholas
Kyungsuk
K
Yum
Jin-Ho
JH
Ahn
Bin
B
Mu
Oliver
O
Plettenburg
Annlouise
A
Gooderman
Sridaran
S
Natesan
Michael S
MS
Strano
D002234:Carbodiimides / Q000737:chemistry; D002942:Circular Dichroism; D005947:Glucose / Q000737:chemistry*; D006358:Hot Temperature; D018625:Microscopy, Atomic Force; D053758:Nanoparticles / Q000737:chemistry; D036103:Nanotechnology / Q000379:methods*; D037742:Nanotubes, Carbon / Q000737:chemistry*; D010777:Photochemistry / Q000379:methods; D011142:Polyvinyl Alcohol; D011485:Protein Binding; D011489:Protein Denaturation; D013056:Spectrophotometry, Ultraviolet; D019265:Spectroscopy, Near-Infrared
D002234:Carbodiimides; D037742:Nanotubes, Carbon; D011142:Polyvinyl Alcohol; D005947:Glucose