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Albumin removal from human serum using surface nanopockets on silica-coated magnetic nanoparticles.

ABSTRACT: Selective removal of albumin from human serum is an essential step prior to proteomic analyses, especially when using mass spectrometry. Here we report stable synthetic nanopockets on magnetic nanoparticle surfaces that bind to human serum albumin (HSA) with high affinity and specificity. The nanopockets are created by templating HSA on 200 nm silica-coated paramagnetic nanoparticles using polymer layers made using 4 organo-silane monomers. These monomers have amino acid-like side chains providing hydrophobic, hydrophilic and H-bonding interactions that closely mimic features of binding sites on antibodies. The binding capacity of the material was 21 mg HSA g-1, and consistently removed ?88% albumin from human serum in multiple repeated use.

SUBMITTER: Bhakta S

PROVIDER: S-EPMC5586046 | biostudies-literature | 2017 Aug

REPOSITORIES: biostudies-literature

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Albumin removal from human serum using surface nanopockets on silica-coated magnetic nanoparticles.

Bhakta Snehasis S Dixit Chandra K CK Bist Itti I Macharia John J Shen Min M Kadimisetty Karteek K He Junkai J Dutta Biswanath B Suib Steven L SL Rusling James F JF

Chemical communications (Cambridge, England) 20170801 66

Selective removal of albumin from human serum is an essential step prior to proteomic analyses, especially when using mass spectrometry. Here we report stable synthetic nanopockets on magnetic nanoparticle surfaces that bind to human serum albumin (HSA) with high affinity and specificity. The nanopockets are created by templating HSA on 200 nm silica-coated paramagnetic nanoparticles using polymer layers made using 4 organo-silane monomers. These monomers have amino acid-like side chains providi ...[more]

PMID: 28770934

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