TY - GEN
T1 - Attenuated-affinity biotin analogs for catch-and-release with streptavidin
AU - Ying, L.
AU - Branchaud, B.
AU - Corry, S.
PY - 2011
Y1 - 2011
N2 - The binding between streptavin and biotin, which is one of the strongest non-covalent interactions known in nature, is used ubiquitously in molecular biology. However, when a biotinylated molecule is captured for testing purposes and cannot be easily removed from the streptavidin-biotin complex, the extreme binding strength is a disadvantage. A successfully engineered streptavin-biotin system for capture and release of sensitive biomaterials must have 1) a strong binding interaction, meaning a low equilibrium binding constant, KD; 2) a fast on-rate, ka, permitting formation of a binding complex within short incubation times; 3) a fast off-rate, kd, permitting rapid re-equilibration of the system upon introducing a competitive binder. Here we present several biotin analogs that have attenuated affinities for streptavidin. Using these compounds, we demonstrate several experimental techniques that were not feasible with prior streptavidin or biotin analogs.
AB - The binding between streptavin and biotin, which is one of the strongest non-covalent interactions known in nature, is used ubiquitously in molecular biology. However, when a biotinylated molecule is captured for testing purposes and cannot be easily removed from the streptavidin-biotin complex, the extreme binding strength is a disadvantage. A successfully engineered streptavin-biotin system for capture and release of sensitive biomaterials must have 1) a strong binding interaction, meaning a low equilibrium binding constant, KD; 2) a fast on-rate, ka, permitting formation of a binding complex within short incubation times; 3) a fast off-rate, kd, permitting rapid re-equilibration of the system upon introducing a competitive binder. Here we present several biotin analogs that have attenuated affinities for streptavidin. Using these compounds, we demonstrate several experimental techniques that were not feasible with prior streptavidin or biotin analogs.
KW - Affinity
KW - Binding
KW - Biotin
KW - Kinetics
KW - Streptavidin
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M3 - Conference contribution
AN - SCOPUS:81455143940
SN - 9781439871386
T3 - Technical Proceedings of the 2011 NSTI Nanotechnology Conference and Expo, NSTI-Nanotech 2011
SP - 151
EP - 154
BT - Technical Proceedings of the 2011 NSTI Nanotechnology Conference and Expo, NSTI-Nanotech 2011
T2 - Nanotechnology 2011: Electronics, Devices, Fabrication, MEMS, Fluidics and Computational - 2011 NSTI Nanotechnology Conference and Expo, NSTI-Nanotech 2011
Y2 - 13 June 2011 through 16 June 2011
ER -