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

Autor: Bhakta S; Department of Chemistry, University of Connecticut, Storrs, Connecticut 06269-3060, USA. Steven.suib@uconn.edu James.rusling@uconn.edu., Dixit CK, Bist I, Macharia J, Shen M, Kadimisetty K, He J, Dutta B, Suib SL, Rusling JF
Jazyk: angličtina
Zdroj: Chemical communications (Cambridge, England) [Chem Commun (Camb)] 2017 Aug 15; Vol. 53 (66), pp. 9254-9257.
DOI: 10.1039/c7cc03412a
Abstrakt: 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.
Databáze: MEDLINE