0000000000309369
AUTHOR
A. M. Rourke
showing 2 related works from this author
Specific interaction of desthiobiotin lipids and water-soluble biotin compounds with streptavidin
1991
As shown for biotin lipids (Ref. 1), the formation of perfect 2-D crystalline streptavidin domains can also be observed in the plane of desthiobiotin lipid monolayers. The binding constant of streptavidin with desthiobiotin (Ka = 5·1013 mol−1) is lower than that with biotin (Ka = 1015 mol−1) (Ref. 2). By adding free biotin into the subphase a competitive replacement and a detaching of the streptavidin domains from the desthiobiotin lipid monolayer takes place. Streptavidin domains built at receptor lipid monolayers are still functional. As could be shown, there are two biotin binding sites at each protein molecule that are fully accessible to biotin (Ref. 1). This can be proven by the inter…
Molecular recognition in biotin-streptavidin systems and analogues at the air-water interface
1992
Abstract Specific interaction between biotin and the protein streptavidin in monolayers of synthetic lipids with biotin headgroups has been shown to lead to formation of highly ordered two-dimensional streptavidin crystals. The same behaviour is observed when using desthiobiotin as lipid headgroup which exhibits a significantly lower binding constant compared with biotin (5 × 10 13 M -1 compared with 10 15 M -1 ). This offers the possibility of detaching competetively the 2D crystalline streptavidin layer by addition of free biotin to the aqueous phase. Use of lipoic acid as lipid headgroup ( K a = 7 × 10 7 M −1 ) leads to formation of small snisotropic protein domains indicating a crystall…