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Interaction of colloidal gold nanoparticles with human blood: effects on particle size and analysis of plasma protein binding profiles.

ABSTRACT: Nanoparticle size and plasma binding profile contribute to a particle's longevity in the bloodstream, which can have important consequences for therapeutic efficacy. In this study an approximate doubling in nanoparticle hydrodynamic size was observed upon in vitro incubation of 30- and 50-nm colloidal gold in human plasma. Plasma proteins that bind the surface of citrate-stabilized gold colloids have been identified. Effects of protein binding on the nanoparticle hydrodynamic size, elements of coagulation, and the complement system have been investigated. The difference in size measurements obtained from dynamic light scattering, electron microscopy, and scanning probe microscopy are also discussed.

SUBMITTER: Dobrovolskaia MA

PROVIDER: S-EPMC3683956 | biostudies-literature | 2009 Jun

REPOSITORIES: biostudies-literature

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Interaction of colloidal gold nanoparticles with human blood: effects on particle size and analysis of plasma protein binding profiles.

Dobrovolskaia Marina A MA Patri Anil K AK Zheng Jiwen J Clogston Jeffrey D JD Ayub Nader N Aggarwal Parag P Neun Barry W BW Hall Jennifer B JB McNeil Scott E SE

Nanomedicine : nanotechnology, biology, and medicine 20081213 2

Nanoparticle size and plasma binding profile contribute to a particle's longevity in the bloodstream, which can have important consequences for therapeutic efficacy. In this study an approximate doubling in nanoparticle hydrodynamic size was observed upon in vitro incubation of 30- and 50-nm colloidal gold in human plasma. Plasma proteins that bind the surface of citrate-stabilized gold colloids have been identified. Effects of protein binding on the nanoparticle hydrodynamic size, elements of c ...[more]

PMID: 19071065

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Project description:The adsorption of amyloidogenic peptides, amyloid beta 1-40 (A?1-40), alpha-synuclein (?-syn), and beta 2 microglobulin (?2m), was attempted over the surface of nano-gold colloidal particles, ranging from d = 10 to 100 nm in diameter (d). The spectroscopic inspection between pH 2 and pH 12 successfully extracted the critical pH point (pHo) at which the color change of the amyloidogenic peptide-coated nano-gold colloids occurred due to aggregation of the nano-gold colloids. The change in surface property caused by the degree of peptide coverage was hypothesized to reflect the ?pHo, which is the difference in pHo between bare gold colloids and peptide coated gold colloids. The coverage ratio (?) for all amyloidogenic peptides over gold colloid of different sizes was extracted by assuming ? = 0 at ?pHo = 0. Remarkably, ? was found to have a nano-gold colloidal size dependence, however, this nano-size dependence was not simply correlated with d. The geometric analysis and simulation of reproducing ? was conducted by assuming a prolate shape of all amyloidogenic peptides. The simulation concluded that a spiking-out orientation of a prolate was required in order to reproduce the extracted ?. The involvement of a secondary layer was suggested; this secondary layer was considered to be due to the networking of the peptides. An extracted average distance of networking between adjacent gold colloids supports the binding of peptides as if they are "entangled" and enclosed in an interfacial distance that was found to be approximately 2 nm. The complex nano-size dependence of ? was explained by available spacing between adjacent prolates. When the secondary layer was formed, A?1-40 and ?-syn possessed a higher affinity to a partially negative nano-gold colloidal surface. However, ?2m peptides tend to interact with each other. This difference was explained by the difference in partial charge distribution over a monomer. Both A?1-40 and ?-syn are considered to have a partial charge (especially ?+) distribution centering around the prolate axis. The ?2m, however, possesses a distorted charge distribution. For a lower ? (i.e., ? <0.5), a prolate was assumed to conduct a gyration motion, maintaining the spiking-out orientation to fill in the unoccupied space with a tilting angle ranging between 5° and 58° depending on the nano-scale and peptide coated to the gold colloid.

Dataset Information

Interaction of colloidal gold nanoparticles with human blood: effects on particle size and analysis of plasma protein binding profiles.

Publications

Interaction of colloidal gold nanoparticles with human blood: effects on particle size and analysis of plasma protein binding profiles.

Similar Datasets

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