Abstract
The mass sensitive sedimentation subtechnique of FFF differs from the flow analogue in two principal ways: Firstly, resolution in sdFFF varies with analyte size to the third power – compared to the first power size dependence for the flow system. Secondly, conversion of sdFFF retention data into mass or size information for the analyte requires knowledge of its density, a quantity that has to be determined separately. Since no such input parameter is required to extract size information from flow FFF data, the sedimentation analogue has obtained a reputation for being less “universal” than its flow counterpart. The present article intends to demonstrate some of the advantages offered by the high mass sensitivity of the sdFFF technique, especially in the design and optimization of bioanalytical processes involving nanoparticles.
This is a preview of subscription content, log in via an institution to check access.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
References
Calvert P (1999) Nanotube composites: a recipe for strength. Nature 399:210–211
Tenne R (2006) Inorganic nanotubes and fullerene-like nanoparticles. Nat Nanotechnol 1:103–111
Klein J (2007) Probing the interactions of proteins and nanoparticles. PNAS 104(7):2029–2030
Gaumet M, Vargas A, Gurny R, Delie F (2008) Nanoparticles for drug delivery: the need for precision in reporting particle size parameters. Eur J Pharm Biopharm 69(1):1–9
Baptista P, Pereira E, Eaton P, Doria G, Miranda A, Gomes I, Quaresma P, Franco R (2008) Gold nanoparticles for the development of clinical diagnosis methods. Anal Bioanal Chem 391:943–950
Ratanathanawongs Williams SK, Runyon JR, Ashames AA (2011) Field-flow fractionation: addressing the nano challenge. Anal Chem 83(3):634–642
Schure MR, Schimpf ME, Schettler PD (2000) Retention – normal mode. In: Schimpf M, Caldwell K, Giddings JC (eds) Field-flow fractionation handbook. Wiley, New York, pp 31–48
Caldwell KD, Li J-M, Li J-T, Dalgleish D (1992) Adsorption behavior of milk proteins on polystyrene latex: a study based on sedimentation field-flow fractionation and dynamic light scattering. J Chromatogr 604:63–71
Li J-T, Caldwell KD (1991) Sedimentation field-flow fractionation in the determination of surface concentration of adsorbed materials. Langmuir 7:2034–2039
Beckett R, Ho J, Yang J, Giddings JC (1991) Measurement of mass and thickness of adsorbed films on colloidal particles by sedimentation field-flow fractionation. Langmuir 7:2040–2047
Langwost B, Caldwell KD (1992) Solid phase immune reactions as monitored by sedimentation field-flow fractionation. Chromatographia 34:317–324
Lee J, Martic PA, Tan JS (1989) Protein adsorption on pluronic copolymer-coated polystyrene particles. J Colloid Interface Sci 131:252–266
Lee JH, Kopecek J, Andrade JD (1989) Protein resistant surfaces prepared by PEO-containing block copolymer surfactants. J Biomed Mater Res 23(3):351–368
Jeon SI, Andrade JD (1992) The steric repulsion properties of polyethylene oxide. Bull Korean Chem Soc 13(3):245–248
Carlsson J, Drevin H, Axén R (1978) Protein thiolation and reversible protein-protein conjugation. N-Succinimidyl 3-(2-pyridyl dithio) propionate, a new heterobifunctional reagent. Biochem J 173(3):723–737
Ho C-H, Limberis L, Caldwell KD, Stewart RJ (1998) A metal-chelating pluronic for immobilization of histidin-tagged proteins at interfaces: immobilization of firefly luciferase on polystyrene beads. Langmuir 14:3889–3894
Andersson M, Elihn K, Fromell K, Caldwell KD (2004) Surface attachment of nanoparticles using oligonucleotides. Colloids Surf B Biointerfaces 34:165–171
Fromell K, Andersson M, Elihn K, Caldwell KD (2005) Nanoparticle decorated surfaces with potential use in glycosylation analysis. Colloids Surf B Biointerfaces 46:84–91
Fromell K (2007) Nanoscale reaction systems. Dissertation, nr. 350 from the Faculty of Science and Technology, Acta Universitatis Upsaliensis, p 11
Tegler LT, Nonglaton G, Buettner F, Caldwell K, Christopeit T, Danielson UH, Fromell K, Gossas T, Larsson A, Longati P, Norberg T, Rampanicker R, Rydberg J, Baltzer L (2011) Powerful protein binders from designed polypeptides and small organic molecules – a general concept for protein recognition. Angew Chemie – int’l ed 50(8):1823–1827
Borchars K, Weber A, Brunner H, Tovar GEM (2005) Microstructured layers of spherical biofunctional core-shell nanoparticles provide enlarged reactive surfaces for protein microarrays. Anal Bioanal Chem 383:738–746
Sanchez-Martin RM, Alexander L, Bradley M (2008) Multifunctionalized biocompatible microspheres for sensing. Ann N Y Acad Sci 1130:207–217
Graham D, Faulds K, Thompson D, McKenzie F, Stokes R, Dalton C, Stevenson R, Alexander J, Garside P, McFarlane E (2009) Functionalized nanoparticles for bioanalysis by SERRS. Biochem Soc Trans 37:697–701
Author information
Authors and Affiliations
Corresponding author
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2012 Springer-Verlag/Wien
About this chapter
Cite this chapter
Caldwell, K.D., Fromell, K. (2012). Multifunctionalized Particles for Biosensor Use. In: Williams, S., Caldwell, K. (eds) Field-Flow Fractionation in Biopolymer Analysis. Springer, Vienna. https://doi.org/10.1007/978-3-7091-0154-4_11
Download citation
DOI: https://doi.org/10.1007/978-3-7091-0154-4_11
Published:
Publisher Name: Springer, Vienna
Print ISBN: 978-3-7091-0153-7
Online ISBN: 978-3-7091-0154-4
eBook Packages: Chemistry and Materials ScienceChemistry and Material Science (R0)