Details
| Originalsprache | Englisch |
|---|---|
| Seiten (von - bis) | 3510-3516 |
| Seitenumfang | 7 |
| Fachzeitschrift | SMALL |
| Jahrgang | 8 |
| Ausgabenummer | 22 |
| Frühes Online-Datum | 23 Aug. 2012 |
| Publikationsstatus | Veröffentlicht - 14 Nov. 2012 |
| Extern publiziert | Ja |
Abstract
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.
ASJC Scopus Sachgebiete
- Biochemie, Genetik und Molekularbiologie (insg.)
- Biotechnologie
- Werkstoffwissenschaften (insg.)
- Biomaterialien
- Chemie (insg.)
- Werkstoffwissenschaften (insg.)
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in: SMALL, Jahrgang 8, Nr. 22, 14.11.2012, S. 3510-3516.
Publikation: Beitrag in Fachzeitschrift › Artikel › Forschung › Peer-Review
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TY - JOUR
T1 - Structure and Function of Glucose Binding Protein–Single Walled Carbon Nanotube Complexe
AU - McNicholas, Thomas P.
AU - Yum, Kyungsuk
AU - Ahn, Jin Ho
AU - Mu, Bin
AU - Plettenburg, Oliver
AU - Gooderman, Annlouise
AU - Natesan, Sridaran
AU - Strano, Michael S.
N1 - Funding Information: We gratefully acknowledge financial support from the Deshpande Center for Technological Innovation and from Sanofi -Aventis.
PY - 2012/11/14
Y1 - 2012/11/14
N2 - 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.
AB - 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.
KW - carbon nanotubes
KW - fluorescence
KW - glucose
KW - periplasmic-binding proteins
UR - http://www.scopus.com/inward/record.url?scp=84869441941&partnerID=8YFLogxK
U2 - 10.1002/smll.201200649
DO - 10.1002/smll.201200649
M3 - Article
C2 - 22915545
AN - SCOPUS:84869441941
VL - 8
SP - 3510
EP - 3516
JO - SMALL
JF - SMALL
SN - 1613-6810
IS - 22
ER -