6533b834fe1ef96bd129d4fd
RESEARCH PRODUCT
Molecular recognition in biotin-streptavidin systems and analogues at the air-water interface
Elmar RumpHelmut RingsdorfA. M. RourkeP.a. SuciM. HoffmannWolfgang Müllersubject
StreptavidinStereochemistrytechnology industry and agricultureMetals and AlloysAqueous two-phase systemSurfaces and InterfacesBinding constantSurfaces Coatings and FilmsElectronic Optical and Magnetic Materialslaw.inventionchemistry.chemical_compoundMolecular recognitionBiotinchemistrylawBiotinylationMonolayerMaterials ChemistryBiophysicslipids (amino acids peptides and proteins)Crystallizationdescription
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 crystallization of streptavidin as already observed with the biotin and desthiobiotinlipids. Interaction of the protein with HABA-lipids ( K a = 10 8 M −1 ) under the same conditions does not lead to domain formation at the air-water interface, although the monolayer behaviour of the HABA lipid is significantly altered by active streptavidin in the subphase.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 1992-04-01 | Thin Solid Films |