skip to main content

This content will become publicly available on June 11, 2016

Title: A novel approach to make homogeneous protease-stable monovalent streptavidin

The interaction between the tetramer streptavidin and biotin is recognized as one of the strongest non-covalent associations. Owing to the tight and specific binding, the streptavidin-biotin system has been used widely for bimolecular labeling, purification, immobilization, and even for targeted delivery of therapeutics drugs. Here, we report a novel approach to make homogeneous monovalent tetramer streptavidin. The purified monovalent protein showed both thermal stability and protease stability. Unexpectedly, we found that two proteases, Proteinase K (PK) and Subtilisin (SU), can efficiently remove the His8-tag from the wild-type subunit without affecting the tetramer architecture of monovalent streptavidin, thus making it more homogeneous. In addition, crystallization was performed to assure the homogeneity of the monovalent protein prepared. Overall, monovalent streptavidin shows increased homogeneity and will likely be valuable for many future applications in a wide range of research areas.
 [1] ;  [2] ;  [2] ;  [3] ;  [4]
  1. Hubei Univ. of Arts and Science (China); Univ. of California, Davis, CA (United States)
  2. Hubei Univ. of Arts and Science (China)
  3. Univ. of California, Davis, CA (United States)
  4. Brookhaven National Lab. (BNL), Upton, NY (United States)
Publication Date:
OSTI Identifier:
Report Number(s):
Journal ID: ISSN 0006-291X; 400412000
Grant/Contract Number:
Accepted Manuscript
Journal Name:
Biochemical and Biophysical Research Communications
Additional Journal Information:
Journal Volume: 463; Journal Issue: 4; Journal ID: ISSN 0006-291X
Research Org:
Brookhaven National Laboratory (BNL), Upton, NY (United States)
Sponsoring Org:
USDOE; National Institute of Health
Country of Publication:
United States
59 BASIC BIOLOGICAL SCIENCES; streptavidin; homogeneity; protease stability