TY - JOUR
T1 - Design of molecular devices based on metalloproteins
T2 - A new approach
AU - Robles-Águila, M. J.
AU - Pérez, K. S.
AU - Stojanoff, V.
AU - Juárez-Santiesteban, H.
AU - Silva-González, R.
AU - Moreno, A.
N1 - Funding Information:
Acknowledgments M.J. R-A thanks for the support and sponsorship as a postdosctoral given by the Mexican Softmater Network (CONACyT). The kind assistance or Dr. A. Mendez-Blas (Laboratory Electrochemical Process) and M.C Laura Serrano (Central Laboratory IFUAP) is higly appreciated. The authors A.M. and R.S.G. gratefully acknowledge financial support from CONACYT Projects Nos. 175924 and 163153, respectively. Preliminary X-ray diffraction experiments were carried out at the National Synchrotron Light Source supported by the NIGMS and DOE under contracts GM-0080 and DE-AC02-98CH10886. The authors acknowledge the TXM picture carried out at the National Synchrotron Light Source by Yu-Chen Karen Chen-Wiegert performed on beamline X8C, Brookhaven National Laboratory. The support from CONACYT MOD-ORD-14-11 PCI-648-0312 is also appreciated.
PY - 2014/3
Y1 - 2014/3
N2 - In this study, cytochrome c and azurin proteins were immobilized onto a porous silicon (PS) surface using the self-assembly technique. The heterostructures were maintained at ambient conditions for several days. Experimental results showed long term stability of proteins in solid state working as electron-transfer devices. Atomic force microscopy showed similar roughness of the surface for both protein heterostructures (14.5 and 11.3 nm, respectively) and globular morphology. Analysis of samples, using scanning electron microscopy, revealed a porous surface of 20-24 nm, whereas cross-section indicated a thickness between 3.6 and 3.8 μm. The fluorescence peak at room temperature, corresponding to blue emission, was observed at 362-550 nm. This is due to the quantum confinement effect through the silicon. Raman measurement showed one Raman's peak, confirming that the prepared sample retained the crystallinity of bulk silicon; immobilization of proteins produced loss of crystallinity. Reflection spectra revealed the PS, changes in the refractive index profile at the interface of the PS, and the modified surface.
AB - In this study, cytochrome c and azurin proteins were immobilized onto a porous silicon (PS) surface using the self-assembly technique. The heterostructures were maintained at ambient conditions for several days. Experimental results showed long term stability of proteins in solid state working as electron-transfer devices. Atomic force microscopy showed similar roughness of the surface for both protein heterostructures (14.5 and 11.3 nm, respectively) and globular morphology. Analysis of samples, using scanning electron microscopy, revealed a porous surface of 20-24 nm, whereas cross-section indicated a thickness between 3.6 and 3.8 μm. The fluorescence peak at room temperature, corresponding to blue emission, was observed at 362-550 nm. This is due to the quantum confinement effect through the silicon. Raman measurement showed one Raman's peak, confirming that the prepared sample retained the crystallinity of bulk silicon; immobilization of proteins produced loss of crystallinity. Reflection spectra revealed the PS, changes in the refractive index profile at the interface of the PS, and the modified surface.
UR - https://www.scopus.com/pages/publications/84894681562
U2 - 10.1007/s10854-014-1734-4
DO - 10.1007/s10854-014-1734-4
M3 - Article
AN - SCOPUS:84894681562
SN - 0957-4522
VL - 25
SP - 1354
EP - 1360
JO - Journal of Materials Science: Materials in Electronics
JF - Journal of Materials Science: Materials in Electronics
IS - 3
ER -