1992
DOI: 10.1016/0142-9612(92)90177-p
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Human serum albumin as a probe for surface conditioning (opsonization) of block copolymer-coated microspheres

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Cited by 82 publications
(31 citation statements)
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“…For example, the amount of HSA adsorbed has been found to increase with increasing surface hydrophobicity. Norman et al have observed that more HSA is adsorbed onto hydrophobic polystyrene particles than those coated with hydrophilic poloxamer or poloxamine block copolymers [20], following the same trend as macrophage uptake [21,22]. Indeed, the group [20] was able to use HSA to probe opsonization of the particles coated with various polymers.…”
Section: Introductionmentioning
confidence: 84%
See 1 more Smart Citation
“…For example, the amount of HSA adsorbed has been found to increase with increasing surface hydrophobicity. Norman et al have observed that more HSA is adsorbed onto hydrophobic polystyrene particles than those coated with hydrophilic poloxamer or poloxamine block copolymers [20], following the same trend as macrophage uptake [21,22]. Indeed, the group [20] was able to use HSA to probe opsonization of the particles coated with various polymers.…”
Section: Introductionmentioning
confidence: 84%
“…HSA, and human monocytes and polymorphonuclear leukocytes (PMNLs). As aforementioned, HSA is the most abundant serum protein and its adsorption has been connected with in vitro phagocytosis and the prediction of in vivo fate of particles [20]. Although IgG exhibits responsive adhesion to PNIPAm nanoparticles [38], this protein usually binds to speci c receptors on phagocytic cells via the Fc portion [41].…”
Section: Introductionmentioning
confidence: 99%
“…In the case of polymeric nanoparticles, although negative charge can be related to a higher uptake [6,31], the surface hydrophobicity appears to be the key factor for opsonization. Nanoparticles prepared from hydrophobic polymers PSt [32], PLA [33], PLGA [34] and PACA [35] undergo important adsorption of Ig, complement proteins and other plasma proteins like albumin, either in vitro or in vivo. To account for these observations, a higher level of protein adsorption on hydrophobic surfaces than on hydrophilic ones has been proposed [36], as well as high affinity of IgG and albumin for hydrophobic regions [28] (van der Waals interactions may be a more accurate description for these ''hydrophobic'' interactions [37]).…”
Section: Surface Propertiesmentioning
confidence: 99%
“…The number of proteins bound to the particles increased with increasing hydrophobicity of the particle surface, as well as with increasing size. Generally, hydrophobic particles are opsonized more quickly than hydrophilic particles, due to the enhanced absorbability of plasma proteins onto the surface of hydrophobic particles [86][87][88][89]. The roles of particle size, surface curvature, and particle surface area in protein binding have also been investigated.…”
Section: Surface Hydrophobicity Evaluation Of Dna Gel Particlesmentioning
confidence: 99%