title: Nematic field transfer in a two-dimensional protein fibril assembly.
abstract: We perform Atomic Force Microscopy and numerical simulations of a bimodal solution containing long, semiflexible β-lactoglobulin fibrils and short, flexible β-lactoglobulin linear aggregates at an air-water interface. Short aggregates orient perpendicular to fibrils at very short distances and preferentially parallel at intermediate distances. At even larger distances an isotropic distribution is observed. Parallel ordering coincides with aggregate stretching: by straightening, small aggregates are able to approach the fibrils within a distance smaller than their radius of gyration. These findings contribute to the understanding of how anisotropic interactions are transferred in two-dimensional bimodal nematic fields of biopolymers at liquid interfaces.
authors.affiliation: Department of Health Sciences & Technology, ETH Zurich, Schmelzbergstrasse 9, 8092 Zurich, Switzerland. ed610@georgetown.edu raffaele.mezzenga@hest.ethz.ch.
authors.forename: Sophia
authors.initials: S
authors.lastname: Jordens
authors.forename: Konrad
authors.initials: K
authors.lastname: Schwenke
authors.forename: Ivan
authors.initials: I
authors.lastname: Usov
authors.forename: Emanuela
authors.initials: E
authors.lastname: Del Gado
authors.forename: Raffaele
authors.initials: R
authors.lastname: Mezzenga
mesh_terms: D000682:Amyloid / Q000737:chemistry*; D016880:Anisotropy; D007782:Lactoglobulins / Q000737:chemistry*; D050866:Liquid Crystals / Q000737:chemistry*
chemical_list: D000682:Amyloid; D007782:Lactoglobulins