title: Single molecule force measurements delineate salt, pH and surface effects on biopolymer adhesion.
abstract: In this paper we probe the influence of surface properties, pH and salt on the adhesion of recombinant spider silk proteins onto solid substrates with single molecule force spectroscopy. A single engineered spider silk protein (monomeric C(16) or dimeric (QAQ)(8)NR3) is covalently bound with one end to an AFM tip, which assures long-time measurements for hours with one and the same protein. The tip with the protein is brought into contact with various substrates at various buffer conditions and then retracted to desorb the protein. We observe a linear dependence of the adhesion force on the concentration of three selected salts (NaCl, NaH(2)PO(4) and NaI) and a Hofmeister series both for anions and cations. As expected, the more hydrophobic C(16) shows a higher adhesion force than (QAQ)(8)NR3, and the adhesion force rises with the hydrophobicity of the substrate. Unexpected is the magnitude of the dependences--we never observe a change of more than 30%, suggesting a surprisingly well-regulated balance between dispersive forces, water-structure-induced forces as well as co-solute-induced forces in biopolymer adhesion.
authors: Physics Department, IMETUM, CeNS and CIPSM, TU München, Garching, Germany.
authors: T
authors: T
authors: Pirzer
authors: M
authors: M
authors: Geisler
authors: T
authors: T
authors: Scheibel
authors: T
authors: T
authors: Hugel
mesh_terms: D000327:Adsorption; D000818:Animals; D005349:Fibroins / Q000737:chemistry*; D006863:Hydrogen-Ion Concentration; D057927:Hydrophobic and Hydrophilic Interactions; D019476:Insect Proteins / Q000737:chemistry*; D018625:Microscopy, Atomic Force; D011994:Recombinant Proteins / Q000737:chemistry; D012492:Salts / Q000737:chemistry; D013112:Spiders / Q000737:chemistry*; D013499:Surface Properties
chemical_list: D019476:Insect Proteins; D011994:Recombinant Proteins; D012492:Salts; D005349:Fibroins