TY - JOUR
T1 - Insights on the emerging biotechnology of histidine-rich peptides
AU - López-Laguna, Hèctor
AU - Voltà-Durán, Eric
AU - Parladé, Eloi
AU - Villaverde, Antonio
AU - Vázquez, Esther
AU - Unzueta, Ugutz
N1 - Publisher Copyright:
© 2021 The Author(s)
PY - 2022/1/1
Y1 - 2022/1/1
N2 - 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.
AB - 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.
KW - Biomaterials
KW - Biosensing
KW - Modular protein
KW - Nanobiotechnology
KW - Recombinant protein
UR - http://www.scopus.com/inward/record.url?scp=85113411010&partnerID=8YFLogxK
UR - https://www.mendeley.com/catalogue/2450096a-18e6-314d-a38d-10ed50e0db8a/
UR - https://portalrecerca.uab.cat/en/publications/307a19a8-8d05-49b9-91e3-43d000d397b0
U2 - 10.1016/j.biotechadv.2021.107817
DO - 10.1016/j.biotechadv.2021.107817
M3 - Review article
C2 - 34418503
AN - SCOPUS:85113411010
SN - 0734-9750
VL - 54
JO - Biotechnology Advances
JF - Biotechnology Advances
M1 - 107817
ER -