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Engineering a disulfide-gated switch in streptavidin enables reversible binding without sacrificing binding affinity. | LitMetric

AI Article Synopsis

  • - The research focuses on improving the binding properties of streptavidin and biotin by introducing disulfide bonds that allow for both strong and reversible binding.
  • - Two engineered versions of streptavidin, M88 and M112, show different effects on binding dynamics: M112 increases the rate of dissociation, while M88 stabilizes the binding.
  • - The ability to control the formation of disulfide bonds in M88 leads to a significantly faster dissociation rate compared to regular streptavidin, opening up new possibilities for applications that require quick ligand release.

Article Abstract

Although high affinity binding between streptavidin and biotin is widely exploited, the accompanying low rate of dissociation prevents its use in many applications where rapid ligand release is also required. To combine extremely tight and reversible binding, we have introduced disulfide bonds into opposite sides of a flexible loop critical for biotin binding, creating streptavidin muteins (M88 and M112) with novel disulfide-switchable binding properties. Crystal structures reveal how each disulfide exerts opposing effects on structure and function. Whereas the disulfide in M112 disrupts the closed conformation to increase k, the disulfide in M88 stabilizes the closed conformation, decreasing k 260-fold relative to streptavidin. The simple and efficient reduction of this disulfide increases k 19,000-fold, thus creating a reversible redox-dependent switch with 70-fold faster dissociation kinetics than streptavidin. The facile control of disulfide formation in M88 will enable the development of many new applications requiring high affinity and reversible binding.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7385176PMC
http://dx.doi.org/10.1038/s41598-020-69357-5DOI Listing

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