title: The position of hydrophobic residues tunes peptide self-assembly.
abstract: The final structure and properties of synthetic peptides mainly depend on their sequence composition and experimental conditions. This work demonstrates that a variation in the positions of hydrophobic residues within a peptide sequence can tune the self-assembly. Techniques employed are atomic force microscopy, transmission electron microscopy and an innovative method based on surface acoustic waves. In addition, a systematic investigation on pH dependence was carried out by utilizing constant experimental parameters.
authors.affiliation: Interdisciplinary Nanoscience Center (iNANO), Gustav Wieds 14, Building 1590, Aarhus C., Denmark. dong@inano.au.dk.
authors.forename: Christian
authors.initials: C
authors.lastname: Bortolini
authors.forename: Lei
authors.initials: L
authors.lastname: Liu
authors.forename: Thomas M A
authors.initials: TM
authors.lastname: Gronewold
authors.forename: Chen
authors.initials: C
authors.lastname: Wang
authors.forename: Flemming
authors.initials: F
authors.lastname: Besenbacher
authors.forename: Mingdong
authors.initials: M
authors.lastname: Dong
mesh_terms: D000595:Amino Acid Sequence; D000596:Amino Acids / Q000737:chemistry*; D002942:Circular Dichroism; D006863:Hydrogen-Ion Concentration; D057927:Hydrophobic and Hydrophilic Interactions; D018625:Microscopy, Atomic Force; D046529:Microscopy, Electron, Transmission; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry*; D017433:Protein Structure, Secondary
chemical_list: D000596:Amino Acids; D010455:Peptides