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Intravenously injected polystyrene nanoparticles, which are prone to rapid sequestration by professional phagocytes, are converted to stealth entities by prior bolus intravenous injection of poloxamine 908. This behaviour is not due to alteration in macrophage phagocytic activity. Laser Doppler anemometry and surface plasmon resonance were used to unravel the mechanisms fundamental to generation of such stealth entities in vivo by poloxamine 908. Electrophoretic mobility of poloxamine pre-coated monodisperse polystyrene nanoparticles in serum, which behave as stealth entities in vivo, was similar to that of uncoated nanoparticles incubated in poloxamine pretreated serum. This observation supported the notion that poloxamine in serum can modify the surface of nanoparticles with similar topography to that of stealth poloxamine pre-coated particles, i.e. with polyoxyethylene chains projected from the surface. Surface plasmon resonance optical phenomenon was used for real-time monitoring of protein^poloxamine interactions and adsorption at the polystyrene interface. It was found that poloxamine can not only adsorb to a serum-modi¢ed surface but in addition poloxamine in serum can form macromolecular complexes with high a⁄nity for adsorption to a polystyrene lattice. A role for serum albumin in surface modi¢cation of nanoparticles by poloxamine 908 is also identi¢ed. Hence, our biophysical observations correlate precisely with the in vivo longevity of uncoated polystyrene nanoparticles in poloxamine pretreated rats. This rational and sensitive biophysical approach has unravelled the probable mechanism fundamental to generation of stealth entities in vivo and therefore has application in the design and nano-engineering of stealth colloidal carriers for optimal biological performance.

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Human serum albumin (HSA) was immobilised on the gold surface of a quartz crystal resonance sensor (QCRS) and exposed to warfarin and diazepam. Distinct decreases in frequency of differing magnitudes were observed upon exposure of the protein to each of the compounds suggesting strongly that a ligand interaction was occurring. Moreover, as sequential exposure in any order was observed to yield distinct repeatable frequency decreases for the ligands indicated, screening for site specific binding may be possible. Identically immobilised bovine serum albumin (BSA) gave no response to either compound.