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Surface Mediated Hierarchical Assemblies of Highly Hydrophobic Phenylalanine‐Based Peptides
Author(s) -
Mayans Enric,
Fabregat Georgina,
Juárez Ruben,
Cativiela Carlos,
Puiggalí Jordi,
Alemán Carlos
Publication year - 2017
Publication title -
chemistryselect
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.437
H-Index - 34
ISSN - 2365-6549
DOI - 10.1002/slct.201601436
Subject(s) - polystyrene , wetting , materials science , contact angle , peptide , chemical engineering , wafer , silicon , polymer chemistry , nanotechnology , chemistry , composite material , polymer , biochemistry , engineering , metallurgy
We report the noticeable control exerted by the surface in the self‐assembly of a highly hydrophobic triphenylalanine peptide with fluorenyl functionalities blocking the two ends. The remarkable differences observed among the polymorphic hierarchical assemblies obtained onto silanized glass, scratched glass, stainless steel, exfoliated mica, silicon wafer, carbon, polytetrafluoroethylene, plasma‐functionalized, polystyrene and nitrocellulose substrates are consequence of the balance between peptide⋅⋅⋅peptide and peptide⋅⋅⋅surface interactions. This balance is greatly influenced by the surface characteristics, as defined by the wettability (hydrophobicity or hydrophilicity) and roughness (degree of flatness and regularity). Furthermore, very stable dendritic structures, in which primary frameworks nucleated from the center grow according to a 4‐fold pseudo‐symmetry branching, have been obtained onto hydrophilic treated polystyrene.