Local pH Gradient Initiated by Light on TiO2 for Light‐Triggered Modulation of Polyhistidine‐Tagged Proteins. Issue 9 (12th August 2016)

• Record Type: Journal Article
• Authors: Andreeva, Daria V.; Melnyk, Inga; Baidukova, Olga; Skorb, Ekaterina V.
• Is Part Of: ChemElectroChem. Volume 3:Issue 9(2016)
• Page Start: 1306
• Page End: 1310
• Publication Date: 2016-08-12
• Subjects: immobilization -- layer-by-layer assembly -- photochemistry -- proteins -- stimuli-responsive materials; Electrochemistry -- Periodicals; 541.37
• DOI: 10.1002/celc.201600268
• Languages: English
• ISSNs: 2196-0216

Abstract

Abstract: A new principle of photo‐assisted spatial desorption of (poly)histidine‐tagged (His‐Tag) proteins on a TiO2 surface is suggested. A semiconductor TiO2 surface is decorated by layer‐by‐layer (LbL) assembly of a strong polyelectrolyte, namely, polystyrene sulfonate (PSS), and nickel–nitrilotriacetic acid (NTA). The PSS/NTA multilayer architecture provides n ‐fold ( n ×NTA) binding efficiency for more precise protein recognition in comparison to existing molecular His‐Tag protein recognition with one‐ and threefold multiplication (1×NTA, 3×NTA). Spatially resolved desorption of proteins is regulated by non‐ photodestructive short‐term low‐intensity light irradiation (<5 mW cm −2 ). The local pH shift on irradiated TiO2 selectively affects the pH‐sensitive NTA/protein complex, but not the LbL assembly of PSS and NTA, which is stable in a broad pH range. Abstract : Light it up : A TiO2 surface is decorated by layer‐by‐layer assembly of polystyrene sulfonate (PSS) and nickel–nitrilotriacetic acid (NTA) to bind (poly)histidine‐tagged (His‐Tag) proteins. Spatially resolved protein desorption is regulated by irradiation with light, causing a local pH shift that affects the pH‐sensitive NTA/protein complex but not the PSS/NTA assembly (see figure).