Journal
BIOTECHNOLOGY ADVANCES
Volume 54, Issue -, Pages -Publisher
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.biotechadv.2021.107817
Keywords
Recombinant protein; Modular protein; Biomaterials; Biosensing; Nanobiotechnology
Categories
Funding
- Agencia Estatal de Investigacion (AEI)
- Fondo Europeo de Desarrollo Regional (FEDER) [BIO2016-76063-R]
- AEI/FEDER, UE
- Instituto de Salud Carlos III (ISCIII) [R01-GM129325]
- AGAUR [2017SGR-229 GRC, 2019FI_B00352]
- CIBER-BBN
- Instituto de Salud Carlos III (ISCIII) - European Regional Development Fund (A way to make Europe) [PI20/00400]
- VI National R&D&I Plan 2008-2011
- Iniciativa Ingenio 2010
- Consolider Program, CIBER Actions
- Instituto de Salud Carlos III
- Ministerio de Ciencia e Innovacion, Spain
- European Regional Development Fund
- ISCIII
- National Institutes of Health [R01-GM129325]
- European Social Fund (ESF investing in your future)
- Office of Cyber Infrastructure and Computational Biology, National Institute of Allergy and Infectious Diseases
- ICREA ACADEMIA award
- [PID2019-105416RB-I00/AEI/10.13039/501100011033]
- [AGAUR 2017SGR-229 GRC]
- [FPU18/04615]
- [CP19/00028]
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The discovery of restriction enzymes in the late 70's enabled the production of functional proteins through recombinant DNA technologies, greatly benefiting biotechnological and pharmaceutical industries. Hexahistidine peptide (H6) has become the gold standard for purification tags in protein production, and histidine-rich peptides are proving to have broad applications in various fields.
In the late 70's, the discovery of the restriction enzymes made possible the biological production of functional proteins by recombinant DNA technologies, a fact that largely empowered both biotechnological and pharmaceutical industries. Short peptides or small protein domains, with specific molecular affinities, were developed as purification tags in downstream processes to separate the target protein from the culture media or cell debris, upon breaking the producing cells. Among these tags, and by exploiting the interactivity of the imidazole ring of histidine residues, the hexahistidine peptide (H6) became a gold standard. Although initially used almost exclusively in protein production, H6 and related His-rich peptides are progressively proving a broad applicability in novel utilities including enzymatic processes, advanced drug delivery systems and diagnosis, through a so far unsuspected adaptation of their binding capabilities. In this context, the coordination of histidine residues and metals confers intriguing functionalities to His-rich sequences useable in the forward-thinking design of protein-based nano-and micro-materials and devices, through strategies that are comprehensively presented here.
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