Functionalization of magnetic nanoparticles with high-binding capacity for affinity separation of therapeutic proteins
Source abstract
Abstract
Magnetic nanoparticles with immobilized metal ligands were prepared for the separation of antibody fragments. First, iron oxide nanoparticles were produced in a solvothermal synthesis using triethylene glycol as solvent and iron(III) acetylacetonate as organic precursor. Via functionalization of the particles with priorly reacted 3-glycidoxypropyltrimethoxysilane and N α,N α-bis(carboxymethyl)-l-lysine (NTA), and charging with Ni2+, magnetic affinity adsorbents were obtained. The particles were applied to separate a His-tagged antibody fragment from a heterogeneous protein mixture of a microbial cultivation supernatant. Binding properties and specificity for purification of the target product ABF D1.3 scFv were optimized regarding the GNTA concentration and were found superior as compared to commercially available systems. A molar ratio of 1:2 Fe2O3:GNTA was most beneficial for the specific purification of the antibody fragment.
Source: openaire · Quality: candidate unverified · Source record ↗
Research context
OpenAlex topics: Monoclonal and Polyclonal Antibodies Research · Protein purification and stability · Nanoparticle-Based Drug Delivery
SciVX discovery tags are terminology-based. OpenAlex topics are source-provided classifications.
References (35)
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