title: Disruption of Escherichia coli amyloid-integrated biofilm formation at the air-liquid interface by a polysorbate surfactant.
abstract: Functional amyloid fibers termed curli contribute to bacterial adhesion and biofilm formation in  Escherichia coli . We discovered that the nonionic surfactant Tween 20 inhibits biofilm formation by uropathogenic  E. coli  at the air-liquid interface, referred to as pellicle formation, and at the solid-liquid interface. At Tween 20 concentrations near and above the critical micelle concentration, the interfacial viscoelastic modulus is reduced to zero as cellular aggregates at the air-liquid interface are locally disconnected and eventually eliminated. Tween 20 does not inhibit the production of curli but prevents curli-integrated film formation. Our results support a model in which the hydrophobic curli fibers associated with bacteria near the air-liquid interface require access to the gas phase to formed strong physical entanglements and to form a network that can support shear stress.
authors.affiliation: Department of Chemical Engineering, Stanford University, Stanford, California 94305, United States.
authors.forename: Cynthia
authors.initials: C
authors.lastname: Wu
authors.forename: Ji Youn
authors.initials: JY
authors.lastname: Lim
authors.forename: Gerald G
authors.initials: GG
authors.lastname: Fuller
authors.forename: Lynette
authors.initials: L
authors.lastname: Cegelski
mesh_terms: D000388:Air; D000682:Amyloid / Q000037:antagonists & inhibitors* / Q000096:biosynthesis / Q000737:chemistry; D018441:Biofilms / Q000187:drug effects*; D004926:Escherichia coli / Q000737:chemistry / Q000187:drug effects* / Q000502:physiology; D011136:Polysorbates / Q000737:chemistry / Q000494:pharmacology*; D013499:Surface Properties; D013501:Surface-Active Agents / Q000737:chemistry / Q000494:pharmacology*
chemical_list: D000682:Amyloid; D011136:Polysorbates; D013501:Surface-Active Agents