Highly efficient purification of 6×histidine-tagged recombinant protein-A by MnFe2O4@NH2@2AB-Ni as a novel and highly stable magnetic nanoparticles

سال انتشار: 1393
نوع سند: مقاله کنفرانسی
زبان: انگلیسی
مشاهده: 435

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شناسه ملی سند علمی:

ICNN05_759

تاریخ نمایه سازی: 30 آبان 1394

چکیده مقاله:

In this study we have developed a simple, cheap, and rapid method for purification of 6×histidine-taggedrecombinant proteins with high yields. The new immobilized metal ion affinity adsorbent was synthesized followingco-precipitation method in order to synthesis of superparamagnetic manganes ferrit nanoparticles, and subsequentlycoated with 3-aminopropyltriethoxysilane (APTES) through a silanization reaction. Manganese ferrite nanoparticlesafforded bidentate ligands as a result of reaction between isatoic anhydride and amino-functionalized MnFe2O4. Thestable surface functionalized nanoparticles were further linked with Ni2+ for purification of 6× His-tagged proteins. Thenanoparticles were approximately 75 nm in size and were stable and had negligible non-specific binding for protein.

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نویسندگان

H Maeimi

Department of Organic Chemistry, Faculty of Chemistry, University of Kashan, Kashan, I,R,Iran

Z Rashid

Department of Organic Chemistry, Faculty of Chemistry, University of Kashan, Kashan, I,R,Iran

M Nazari

Nanobiotechnology Research Center, Avicenna Research Institute, ACECR, Tehran, Iran

M.R Nejadmoghaddam

Nanobiotechnology Research Center, Avicenna Research Institute, ACECR, Tehran, Iran