TY - JOUR
T1 - Polypyrrole-supported membrane proteins for bio-inspired ion channels
AU - Pérez-Madrigal, Maria M.
AU - Del Valle, Luis J.
AU - Armelin, Elaine
AU - Michaux, Catherine
AU - Roussel, Guillaume
AU - Perpète, Eric A.
AU - Alemán, Carlos
PY - 2015
Y1 - 2015
N2 - Biomedical platforms constructed by immobilizing membrane proteins in matrixes made of synthetic organic polymers is a challenge because the structure and function of these proteins are affected by environmental conditions. In this work, an operative composite that regulates the diffusion of alkali ions has been prepared by functionalizing a supporting matrix made of poly(N-methylpyrrole) (PNMPy) with a β-barrel membrane protein (Omp2a) that forms channels and pores. The protein has been unequivocally identified in the composite, and its structure has been shown to remain unaltered. The PNMPy-Omp2a platform fulfills properties typically associated with functional bio-interfaces with biomedical applications (e.g., biocompatibility, biodegrabadility, and hydrophilicity). The functionality of the immobilized protein has been examined by studying the passive ion transport response in the presence of electrolytic solutions with Na+ and K+ concentrations close to those found in blood. Although the behavior of PNMPy and PNMPy-Omp2a is very similar for solutions with very low concentration, the resistance of the latter decreases drastically when the concentration of ions increases to ∼100 mM. This reduction reflects an enhanced ion exchange between the biocomposite and the electrolytic medium, which is not observed in PNMPy, evidencing that PNMPy-Omp2a is particularly well suited to prepare bioinspired channels and smart biosensors.
AB - Biomedical platforms constructed by immobilizing membrane proteins in matrixes made of synthetic organic polymers is a challenge because the structure and function of these proteins are affected by environmental conditions. In this work, an operative composite that regulates the diffusion of alkali ions has been prepared by functionalizing a supporting matrix made of poly(N-methylpyrrole) (PNMPy) with a β-barrel membrane protein (Omp2a) that forms channels and pores. The protein has been unequivocally identified in the composite, and its structure has been shown to remain unaltered. The PNMPy-Omp2a platform fulfills properties typically associated with functional bio-interfaces with biomedical applications (e.g., biocompatibility, biodegrabadility, and hydrophilicity). The functionality of the immobilized protein has been examined by studying the passive ion transport response in the presence of electrolytic solutions with Na+ and K+ concentrations close to those found in blood. Although the behavior of PNMPy and PNMPy-Omp2a is very similar for solutions with very low concentration, the resistance of the latter decreases drastically when the concentration of ions increases to ∼100 mM. This reduction reflects an enhanced ion exchange between the biocomposite and the electrolytic medium, which is not observed in PNMPy, evidencing that PNMPy-Omp2a is particularly well suited to prepare bioinspired channels and smart biosensors.
KW - bioinspired channels
KW - electroactive polymer
KW - electrochemical impedance spectroscopy
KW - functional bio-interfaces
KW - ion exchange
UR - http://www.scopus.com/inward/record.url?scp=84921819573&partnerID=8YFLogxK
U2 - 10.1021/am507142f
DO - 10.1021/am507142f
M3 - Article
AN - SCOPUS:84921819573
SN - 1944-8244
VL - 7
SP - 1632
EP - 1643
JO - ACS Applied Materials & Interfaces
JF - ACS Applied Materials & Interfaces
IS - 3
ER -