scholarly journals Computationally Selected Epitopes: Integrated Approaches Toward High‐Affinity Artificial Protein Binders Obtained via Computationally Simulated Epitopes for Protein Recognition (Adv. Funct. Mater. 15/2019)

2019 ◽  
Vol 29 (15) ◽  
pp. 1970094
Author(s):  
Zeynep Altintas ◽  
Aref Takiden ◽  
Tillmann Utesch ◽  
Maria A. Mroginski ◽  
Bianca Schmid ◽  
...  
Keyword(s):  
Protein Recognition ◽  
High Affinity ◽  
Protein Binders ◽  
Integrated Approaches ◽  
Artificial Protein

Integrated Approaches Toward High‐Affinity Artificial Protein Binders Obtained via Computationally Simulated Epitopes for Protein Recognition

2019 ◽  
Vol 29 (15) ◽  
pp. 1807332 ◽  
Author(s):  
Zeynep Altintas ◽  
Aref Takiden ◽  
Tillmann Utesch ◽  
Maria A. Mroginski ◽  
Bianca Schmid ◽  
...  
Keyword(s):  
Protein Recognition ◽  
High Affinity ◽  
Protein Binders ◽  
Integrated Approaches ◽  
Artificial Protein

Powerful Protein Binders from Designed Polypeptides and Small Organic Molecules-A General Concept for Protein Recognition

2011 ◽  
Vol 123 (8) ◽  
pp. 1863-1867 ◽  
Author(s):  
Lotta T. Tegler ◽  
Guillaume Nonglaton ◽  
Frank Büttner ◽  
Karin Caldwell ◽  
Tony Christopeit ◽  
...  
Keyword(s):  
Organic Molecules ◽  
General Concept ◽  
Protein Recognition ◽  
Small Organic Molecules ◽  
Protein Binders

Optical microchips based on high-affinity recombinant protein binders—Human serum albumin detection in urine

2018 ◽  
Vol 272 ◽  
pp. 441-447 ◽  
Author(s):  
Alena Semeradtova ◽  
Marcel Stofik ◽  
Lucie Vankova ◽  
Petr Maly ◽  
Ondrej Stanek ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Recombinant Protein ◽  
Serum Albumin ◽  
Human Serum ◽  
High Affinity ◽  
Protein Binders

Protein recognition by cucurbit[6]uril: high affinity N-terminal complexation

2021 ◽  
Author(s):  
Kiefer O. Ramberg ◽  
Sylvain Engilberge ◽  
Francesca Guagnini ◽  
Peter B. Crowley
Keyword(s):  
Protein Recognition ◽  
High Affinity

Cucurbit[6]uril can recognize and bind the N-terminal Met-Lys motif in proteins. However, the intrapeptide Met-Lys feature does not bind the macrocycle.

scholarly journals Protein recognition by bivalent, ‘turn-on’ fluorescent molecular probes

2015 ◽  
Vol 6 (10) ◽  
pp. 5419-5425 ◽  
Author(s):  
Linor Unger-Angel ◽  
Bhimsen Rout ◽  
Tal Ilani ◽  
Miriam Eisenstein ◽  
Leila Motiei ◽  
...  
Keyword(s):  
Signal To Noise Ratio ◽  
Molecular Probes ◽  
Fluorescence Probes ◽  
Protein Recognition ◽  
High Signal ◽  
Thiazole Orange ◽  
Turn On ◽  
Intercalating Dye ◽  
Protein Binders ◽  
Fluorescent Molecular Probes

The selective and sensitive identification of different proteins becomes possible by modifying the known intercalating dye, thiazole orange, with two protein binders. These ‘turn-on’ fluorescence probes enable the identification of acetylcholinesterase, glutathione-s-transferases and avidin with high affinity, specificity, and high signal-to-noise ratio.

Powerful Protein Binders from Designed Polypeptides and Small Organic Molecules-A General Concept for Protein Recognition

2011 ◽  
Vol 50 (8) ◽  
pp. 1823-1827 ◽  
Author(s):  
Lotta T. Tegler ◽  
Guillaume Nonglaton ◽  
Frank Büttner ◽  
Karin Caldwell ◽  
Tony Christopeit ◽  
...  
Keyword(s):  
Organic Molecules ◽  
General Concept ◽  
Protein Recognition ◽  
Small Organic Molecules ◽  
Protein Binders

scholarly journals Light-responsive monobodies for dynamic control of customizable protein binding

2020 ◽  
Author(s):  
César Carrasco-López ◽  
Evan M. Zhao ◽  
Agnieszka A. Gil ◽  
Nathan Alam ◽  
Jared E. Toettcher ◽  
...  
Keyword(s):  
Protein Interactions ◽  
Dynamic Control ◽  
Binding Activity ◽  
Sh2 Domain ◽  
Protein Protein Interactions ◽  
High Affinity ◽  
Protein Binders ◽  
Basic And Applied Research

ABSTRACTCustomizable, high affinity protein-protein interactions, such as those mediated by antibodies and antibody-like molecules, are invaluable to basic and applied research and have become pillars for modern therapeutics. The ability to reversibly control the binding activity of these proteins to their targets on demand would significantly expand their applications in biotechnology, medicine, and research. Here we present, as proof-of-principle, a light-controlled monobody (OptoMB) that works in vitro and in vivo, whose affinity for its SH2-domain target exhibits a 300-fold shift in binding affinity upon illumination. We demonstrate that our αSH2-OptoMB can be used to purify SH2-tagged proteins directly from crude E. coli extract, achieving 99.8% purity and over 40% yield in a single purification step. This OptoMB belongs to a new class of light-sensitive protein binders we call OptoBinders (OptoBNDRs) which, by virtue of their ability to be designed to bind any protein of interest, have the potential to find new powerful applications as light-switchable binders of untagged proteins with high affinity and selectivity, and with the temporal and spatial precision afforded by light.

Cell immunocapture microfluidic chip based on high-affinity recombinant protein binders

2021 ◽  
Vol 172 ◽  
pp. 112784
Author(s):  
Jiří Smejkal ◽  
Petr Malý ◽  
Milan Kuchař ◽  
Natalya Panova ◽  
Alena Semerádtová ◽  
...  
Keyword(s):  
Recombinant Protein ◽  
Microfluidic Chip ◽  
High Affinity ◽  
Protein Binders
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