title: Stabilization of peptide fibrils by hydrophobic interaction.
abstract: Hydrophobic interactions play an important role in assembly processes in aqueous environments. In case of peptide amphiphiles, hydrophobicity is combined with hydrogen bonding to yield well-defined peptide-based aggregates. Here, we report a systematic study after the role of hydrophobic interactions on both stabilization and morphology of a peptide fibrillar assembly. For this purpose, alkyl tails were connected to a known beta-sheet forming peptide with the sequence KTVIIE. The introduction of n-alkyl groups induced thermal stability to the assemblies without affecting the morphology of the peptide aggregates.
authors.affiliation: Organic Chemistry, Institute for Molecules and Materials and Center for Molecular and Biomolecular Informatics, NCMLS, Radboud University Nijmegen, Toernooiveld 1- Huygens Building 03.016, 6525 ED Nijmegen, The Netherlands.
authors.forename: Joris T
authors.initials: JT
authors.lastname: Meijer
authors.forename: Marjolijn
authors.initials: M
authors.lastname: Roeters
authors.forename: Valentina
authors.initials: V
authors.lastname: Viola
authors.forename: Dennis W P M
authors.initials: DW
authors.lastname: Löwik
authors.forename: Gert
authors.initials: G
authors.lastname: Vriend
authors.forename: Jan C M
authors.initials: JC
authors.lastname: van Hest
mesh_terms: D000595:Amino Acid Sequence; D002942:Circular Dichroism; D057927:Hydrophobic and Hydrophilic Interactions; D046529:Microscopy, Electron, Transmission; D010455:Peptides / Q000138:chemical synthesis / Q000737:chemistry*; D013696:Temperature
chemical_list: D010455:Peptides