title: Capturing Conformation-Dependent Molecule-Surface Interactions When Surface Chemistry Is Heterogeneous.
abstract: Molecular building blocks, such as carbon nanotubes and DNA origami, can be fully integrated into electronic and optical devices if they can be assembled on solid surfaces using biomolecular interactions. However, the conformation and functionality of biomolecules depend strongly on the local chemical environment, which is highly heterogeneous near a surface. To help realize the potential of biomolecular self-assembly, we introduce here a technique to spatially map molecular conformations and adsorption, based on single-molecule fluorescence microscopy. On a deliberately patterned surface, with regions of varying hydrophobicity, we characterized the conformations of adsorbed helicogenic alanine-lysine copeptides using Förster resonance energy transfer. The peptides adopted helical conformations on hydrophilic regions of the surface more often than on hydrophobic regions, consistent with previous ensemble-averaged observations of α-helix surface stability. Interestingly, this dependence on surface chemistry was not due to surface-induced unfolding, as the apparent folding and unfolding dynamics were usually much slower than desorption. The most significant effect of surface chemistry was on the adsorption rate of molecules as a function of their initial conformational state. In particular, regions with higher adsorption rates attracted more molecules in compact, disordered coil states, and this difference in adsorption rates dominated the average conformation of the ensemble. The correlation between adsorption rate and average conformation was also observed on nominally uniform surfaces. Spatial variations in the functional state of adsorbed molecules would strongly affect the success rates of surface-based molecular assembly and can be fully understood using the approach developed in this work.
authors.affiliation: Department of Chemical and Biological Engineering, University of Colorado Boulder, Boulder, Colorado 80309, United States.
authors.forename: Joshua N
authors.initials: JN
authors.lastname: Mabry
authors.affiliation: Department of Chemical and Biological Engineering, University of Colorado Boulder, Boulder, Colorado 80309, United States.
authors.forename: Mark
authors.initials: M
authors.lastname: Kastantin
authors.affiliation: Department of Chemical and Biological Engineering, University of Colorado Boulder, Boulder, Colorado 80309, United States.
authors.forename: Daniel K
authors.initials: DK
authors.lastname: Schwartz
mesh_terms: D000327:Adsorption; D000595:Amino Acid Sequence; D031541:Fluorescence Resonance Energy Transfer; D057927:Hydrophobic and Hydrophilic Interactions; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry*; D011487:Protein Conformation; D017510:Protein Folding
chemical_list: D010455:Peptides
keywords: hydrophobicity; self-assembly; single-molecule; surface chemistry; α-helix