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Protease‐resistant streptavidin for interaction proteomics

open access: yesMolecular Systems Biology, 2020
Streptavidin-mediated enrichment is a powerful strategy to identify biotinylated biomolecules and their interaction partners; however, intense streptavidin-derived peptides impede protein identification by mass spectrometry. Here, we present an approach to chemically modify streptavidin, thus rendering it resistant to proteolysis by trypsin and LysC ...
Mahmoud-Reza Rafiee   +10 more
doaj   +5 more sources

Streptavidin Coverage on Biotinylated Surfaces [PDF]

open access: yesACS Applied Materials & Interfaces, 2021
Biosensors and other biological platform technologies require the functionalization of their surface with receptors to enhance affinity and selectivity. Control over the functionalization density is required to tune the platform's properties. Streptavidin (SAv) monolayers are widely used to immobilize biotinylated proteins, receptors, and DNA.
P. H. Erik Hamming, Jurriaan Huskens
openaire   +5 more sources

Production of mutant streptavidin protein and investigation of its effect on the performance of streptavidin. [PDF]

open access: yesIranian journal of basic medical sciences, 2023
Streptavidin is a versatile protein in cell science. The tetramer structure of streptavidin plays a key role in this binding, but this form interferes with some assays. If monomer streptavidin is still capable of binding to biotin, it can overcome the limitations of the streptavidin application. So, we examined the elimination of tryptophan 120 and its
Elham Didevara   +3 more
openaire   +3 more sources

The Crystal Structure of Monovalent Streptavidin [PDF]

open access: yesScientific Reports, 2016
AbstractThe strong interaction between streptavidin (SA) and biotin is widely utilized in biotechnological applications. A SA variant, monovalent SA, was developed with a single and high affinity biotin-binding site within the intact tetramer. However, its structural characterization remains undetermined.
Zhang, Min   +3 more
openaire   +6 more sources

Streptavidin-Hosted Organocatalytic Aldol Addition [PDF]

open access: yesMolecules, 2020
In this report, the streptavidin-biotin technology was applied to enable organocatalytic aldol addition. By attaching pyrrolidine to the valeric motif of biotin and introducing it to streptavidin (Sav), a protein-based organocatalytic system was created, and the aldol addition of acetone with p-nitrobenzaldehyde was tested.
Nicolò Santi   +2 more
openaire   +5 more sources

Co-Streptavidin Precipitation [PDF]

open access: yesBIO-PROTOCOL, 2013
Co-Streptavidin Precipitation (Co-SP) is a method to pull down protein partners of a protein of interest tagged with the streptavidin binding protein domain, and using streptavidin columns that specifically bind to Streptavidin Binding Protein (SBP) in order to test the protein-protein interactions.
Pierre Ferrier   +2 more
openaire   +4 more sources

Thermophoresis: The Case of Streptavidin and Biotin [PDF]

open access: yesPolymers, 2020
Thermophoretic behavior of a free protein changes upon ligand binding and gives access to information on the binding constants. The Soret effect has also been proven to be a promising tool to gain information on the hydration layer, as the temperature dependence of the thermodiffusion behavior is sensitive to solute–solvent interactions.
Doreen Niether   +5 more
openaire   +6 more sources

Postsecretory modifications of streptavidin [PDF]

open access: yesBiochemical Journal, 1989
Streptavidin, an extracellular biotin-binding protein from Streptomyces avidinii, exhibits a multiplicity in its electrophoretic mobility pattern which depends both upon the conditions for growth of the bacterium and upon the protocol used in the purification of the protein.
Y Hiller   +3 more
openaire   +3 more sources

Thermodiffusion as a probe of protein hydration for streptavidin and the streptavidin-biotin complex [PDF]

open access: yesAIP Conference Proceedings, 2018
Molecular recognition via protein–ligand interactions is of fundamental importance to numerous processes in living organisms. Microscale thermophoresis (MST) uses the sensitivity of the thermophoretic response upon ligand binding to access information on the reaction kinetics.
Niether, Doreen   +6 more
openaire   +3 more sources

Monovalent Streptavidin that Senses Oligonucleotides [PDF]

open access: yesAngewandte Chemie, 2013
We report a straightforward chemical route to monovalent streptavidin, a valuable reagent for imaging. The one-step process is based on a (tris)biotinylated-oligonucleotide blocking three of streptavidin’s four biotin binding sites. Further, the complex is highly sensitive to single-base differences - whereby perfectly matched oligonucleotides trigger ...
Jingxian Wang   +3 more
openaire   +3 more sources

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