title: Engineering mechanosensitive multivalent receptor-ligand interactions: why the nanolinker regions of bacterial adhesins matter.
abstract: Inspired by bacterial adhesins, we present a promising strategy of how to engineer peptides to probe various mechanical strains of extracellular matrix fibers. Functional sequence alignment of bacterial adhesins reveals that the bacterial linkers connecting the multivalent binding motifs recognizing fibronectin show considerable heterogeneity in length. Their length regulates the tunable affinities for fibronectin fibrils when stretched into different mechanical strain states. This platform has potential applications in probing extracellular matrix fiber strains in tissues.
authors.affiliation: Department of Health Sciences and Technology, ETH Zurich, CH-8093, Zürich, Switzerland.
authors.forename: Samuel
authors.initials: S
authors.lastname: Hertig
authors.forename: Mamta
authors.initials: M
authors.lastname: Chabria
authors.forename: Viola
authors.initials: V
authors.lastname: Vogel
mesh_terms: D018829:Adhesins, Bacterial / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D000595:Amino Acid Sequence; D001696:Biomechanical Phenomena; D005353:Fibronectins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D008024:Ligands; D008958:Models, Molecular; D056004:Molecular Dynamics Simulation; D008969:Molecular Sequence Data; D036103:Nanotechnology; D015202:Protein Engineering; D054730:Protein Interaction Domains and Motifs; D017386:Sequence Homology, Amino Acid
chemical_list: D018829:Adhesins, Bacterial; D005353:Fibronectins; D008024:Ligands; C078635:fibronectin-binding proteins, bacterial