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https://hdl.handle.net/1822/87227
Título: | Recombinant protein purification and immobilization strategies based on peptides with dual affinity to iron oxide and silica |
Autor(es): | Aguiar, Tatiana Quinta Domingues, Lucília |
Palavras-chave: | protein purification/immobilization affinity tags solid-binding peptides iron oxide silica |
Data: | Nov-2023 |
Editora: | Wiley-Blackwell |
Revista: | Biotechnology Journal |
Citação: | Aguiar, T. Q., & Domingues, L. (2023, July 28). Recombinant protein purification and immobilization strategies based on peptides with dual affinity to iron oxide and silica. Biotechnology Journal. Wiley. http://doi.org/10.1002/biot.202300152 |
Resumo(s): | Iron oxide and silica-based materials have emerged as attractive protein purification and immobilization matrices. His6 has been reported as an effective affinity tag for both iron oxide and silica. Here, the silica-binding tags CotB1p and Car9 were shown to work as effectively as iron oxide-binding tags. Using EGFP as a model protein, commercially available bare iron oxide (BIONs) or silicon dioxide (BSiNs) nanoparticles as low-cost purification/immobilization matrices, and non-hazardous and mild binding and elution conditions, adsorption and desorption studies were performed with lysates from Escherichia coli-producing cells to compare the performance of these dual-affinity tags. Under the conditions tested, the His6 tag stood out as the best-performing tag, followed by CotB1p. Our findings concluded the promising combination of these tags, BIONs and BSiNs for one-step purification of recombinant proteins, and two-step purification and immobilization of recombinant proteins without intermediate buffer exchange. This proof of concept work set the ground for future evaluation of these purification and immobilization strategies using other proteins with different properties, which will be of interest to expand their utility and applicability. This article is protected by copyright. All rights reserved |
Tipo: | Artigo |
URI: | https://hdl.handle.net/1822/87227 |
DOI: | 10.1002/biot.202300152 |
ISSN: | 1860-6768 |
Versão da editora: | http://onlinelibrary.wiley.com/journal/10.1002/(ISSN)1860-7314 |
Arbitragem científica: | yes |
Acesso: | Acesso restrito UMinho |
Aparece nas coleções: | CEB - Publicações em Revistas/Séries Internacionais / Publications in International Journals/Series |
Ficheiros deste registo:
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document_56350_1.pdf Acesso restrito! | 1,23 MB | Adobe PDF | Ver/Abrir |