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Designed Ankyrin Repeat Proteins: A New Class of Viral Entry Inhibitors

Designed ankyrin repeat proteins (DARPins) are engineered proteins comprising consensus designed ankyrin repeats as scaffold. Tightly packed repeats form a continuous hydrophobic core and a large groove-like solvent-accessible surface that creates a binding surface. DARPin domains recognizing a targ...

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Detalles Bibliográficos
Autores principales: Walser, Marcel, Mayor, Jennifer, Rothenberger, Sylvia
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9611651/
https://www.ncbi.nlm.nih.gov/pubmed/36298797
http://dx.doi.org/10.3390/v14102242
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author Walser, Marcel
Mayor, Jennifer
Rothenberger, Sylvia
author_facet Walser, Marcel
Mayor, Jennifer
Rothenberger, Sylvia
author_sort Walser, Marcel
collection PubMed
description Designed ankyrin repeat proteins (DARPins) are engineered proteins comprising consensus designed ankyrin repeats as scaffold. Tightly packed repeats form a continuous hydrophobic core and a large groove-like solvent-accessible surface that creates a binding surface. DARPin domains recognizing a target of interest with high specificity and affinity can be generated using a synthetic combinatorial library and in vitro selection methods. They can be linked together in a single molecule to build multispecific and multifunctional proteins without affecting expression or function. The modular architecture of DARPins offers unprecedented possibilities of design and opens avenues for innovative antiviral strategies.
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spelling pubmed-96116512022-10-28 Designed Ankyrin Repeat Proteins: A New Class of Viral Entry Inhibitors Walser, Marcel Mayor, Jennifer Rothenberger, Sylvia Viruses Review Designed ankyrin repeat proteins (DARPins) are engineered proteins comprising consensus designed ankyrin repeats as scaffold. Tightly packed repeats form a continuous hydrophobic core and a large groove-like solvent-accessible surface that creates a binding surface. DARPin domains recognizing a target of interest with high specificity and affinity can be generated using a synthetic combinatorial library and in vitro selection methods. They can be linked together in a single molecule to build multispecific and multifunctional proteins without affecting expression or function. The modular architecture of DARPins offers unprecedented possibilities of design and opens avenues for innovative antiviral strategies. MDPI 2022-10-12 /pmc/articles/PMC9611651/ /pubmed/36298797 http://dx.doi.org/10.3390/v14102242 Text en © 2022 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Review
Walser, Marcel
Mayor, Jennifer
Rothenberger, Sylvia
Designed Ankyrin Repeat Proteins: A New Class of Viral Entry Inhibitors
title Designed Ankyrin Repeat Proteins: A New Class of Viral Entry Inhibitors
title_full Designed Ankyrin Repeat Proteins: A New Class of Viral Entry Inhibitors
title_fullStr Designed Ankyrin Repeat Proteins: A New Class of Viral Entry Inhibitors
title_full_unstemmed Designed Ankyrin Repeat Proteins: A New Class of Viral Entry Inhibitors
title_short Designed Ankyrin Repeat Proteins: A New Class of Viral Entry Inhibitors
title_sort designed ankyrin repeat proteins: a new class of viral entry inhibitors
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9611651/
https://www.ncbi.nlm.nih.gov/pubmed/36298797
http://dx.doi.org/10.3390/v14102242
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