TY - JOUR
T1 - Surface Characterization and in situ Protein Adsorption Studies on Carbene-Modified Polymers
AU - Nelson, Geoffrey W.
AU - Parker, Emily M.
AU - Singh, Kulveer
AU - Blanford, Christopher F.
AU - Moloney, Mark G.
AU - Foord, John S.
N1 - Primary funding for the project was provided by C.F.B. (EP/G00434X/1), J.S.F., and M.G.M.
PY - 2015/9/21
Y1 - 2015/9/21
N2 - Polystyrene thin films were functionalized using a facile two-step chemical protocol involving carbene insertion followed by azo-coupling, permitting the introduction of a range of chemical functional groups, including aniline, hexyl, amine, carboxyl, phenyl, phosphonate diester, and ethylene glycol. X-ray photoelectron spectroscopy (XPS) confirmed the success of the two-step chemical modification with a grafting density of at least 1/10th of the typical loading density (1014–1015) of a self-assembled monolayer (SAM). In situ, real-time quartz crystal microbalance with dissipation (QCM-D) studies show that the dynamics of binding of bovine serum albumin (BSA) are different at each modified surface. Mass, viscoelastic, and kinetic data were analyzed, and compared to cheminformatic descriptors (i.e., c log P, polar surface area) typically used for drug discovery. Results show that functionalities may either resist or adsorb BSA, and uniquely influence its adsorption dynamics. It is concluded that carbene-based surface modification can usefully influence BSA binding dynamics in a manner consistent with, and more robust than, traditional systems based on SAM chemistry.
AB - Polystyrene thin films were functionalized using a facile two-step chemical protocol involving carbene insertion followed by azo-coupling, permitting the introduction of a range of chemical functional groups, including aniline, hexyl, amine, carboxyl, phenyl, phosphonate diester, and ethylene glycol. X-ray photoelectron spectroscopy (XPS) confirmed the success of the two-step chemical modification with a grafting density of at least 1/10th of the typical loading density (1014–1015) of a self-assembled monolayer (SAM). In situ, real-time quartz crystal microbalance with dissipation (QCM-D) studies show that the dynamics of binding of bovine serum albumin (BSA) are different at each modified surface. Mass, viscoelastic, and kinetic data were analyzed, and compared to cheminformatic descriptors (i.e., c log P, polar surface area) typically used for drug discovery. Results show that functionalities may either resist or adsorb BSA, and uniquely influence its adsorption dynamics. It is concluded that carbene-based surface modification can usefully influence BSA binding dynamics in a manner consistent with, and more robust than, traditional systems based on SAM chemistry.
U2 - 10.1021/acs.langmuir.5b01644
DO - 10.1021/acs.langmuir.5b01644
M3 - Article
SN - 0743-7463
VL - 31
SP - 11086
EP - 11096
JO - Langmuir
JF - Langmuir
IS - 40
ER -