A comparison between dual polarization interferometry (DPI) and surface plasmon resonance (SPR) for protein adsorption studies Export

@article{citeulike:5973672, abstract = {This work was performed with the aim of comparing protein adsorption results obtained from the recently developed dual polarization interferometry (DPI) with the well-established surface plasmon resonance (SPR) technique. Both techniques use an evanescent field as the sensing element but completely different methods to calculate the adsorbed mass. As a test system we used adsorption of the lipase from Thermomyces lanuginosus (TLL) on C18 surfaces. The adsorbed amount calculated with both techniques is in good agreement, with both adsorption isotherms saturating at 1.30–1.35 mg/m 2 at TLL concentrations of 1000 nM and above. Therefore, this supports the use of both SPR and DPI as tools for studying protein adsorption, which is very important when comparing adsorption data obtained from the use different techniques. Due to the spot sensing in SPR, this technique is recommended for initial kinetic studies, whereas DPI is more accurate when the refractive index and thickness of the adsorbed layer is of more interest.}, author = {Sonesson, A. and Callisen, T. and Brismar, H. and Elofsson, U.}, citeulike-article-id = {5973672}, citeulike-linkout-0 = {http://dx.doi.org/10.1016/j.colsurfb.2006.10.028}, citeulike-linkout-1 = {http://linkinghub.elsevier.com/retrieve/pii/S0927776506003493}, day = {15}, doi = {10.1016/j.colsurfb.2006.10.028}, issn = {09277765}, journal = {Colloids and Surfaces B: Biointerfaces}, keywords = {biosensor, dpi, experiment, farfield, kth\_papers, protein, surface\_plasmon\_resonance}, month = {February}, number = {2}, pages = {236--240}, posted-at = {2009-10-20 12:44:54}, priority = {2}, title = {A comparison between dual polarization interferometry (DPI) and surface plasmon resonance (SPR) for protein adsorption studies}, url = {http://dx.doi.org/10.1016/j.colsurfb.2006.10.028}, volume = {54}, year = {2007} }

TY - JOUR ID - citeulike:5973672 L3 - citeulike-article-id:5973672 N2 - This work was performed with the aim of comparing protein adsorption results obtained from the recently developed dual polarization interferometry (DPI) with the well-established surface plasmon resonance (SPR) technique. Both techniques use an evanescent field as the sensing element but completely different methods to calculate the adsorbed mass. As a test system we used adsorption of the lipase from Thermomyces lanuginosus (TLL) on C18 surfaces. The adsorbed amount calculated with both techniques is in good agreement, with both adsorption isotherms saturating at 1.30–1.35 mg/m 2 at TLL concentrations of 1000 nM and above. Therefore, this supports the use of both SPR and DPI as tools for studying protein adsorption, which is very important when comparing adsorption data obtained from the use different techniques. Due to the spot sensing in SPR, this technique is recommended for initial kinetic studies, whereas DPI is more accurate when the refractive index and thickness of the adsorbed layer is of more interest. IS - 2 JF - Colloids and Surfaces B: Biointerfaces SN - 09277765 EP - 240 TI - A comparison between dual polarization interferometry (DPI) and surface plasmon resonance (SPR) for protein adsorption studies VL - 54 SP - 236 KW - biosensor KW - dpi KW - experiment KW - farfield KW - kth_papers KW - protein KW - surface_plasmon_resonance AU - Sonesson, A AU - Callisen, T AU - Brismar, H AU - Elofsson, U PY - 2007/02/15/ UR - http://dx.doi.org/10.1016/j.colsurfb.2006.10.028 ER -