Hydrophobic interactions play an important role in assembly processes in aqueous environments. In case of peptideamphiphiles, 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 morphologyof a peptide fibrillar assembly. For this purpose, alkyl tails were connected to a known
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-sheet forming peptide withthe sequence KTVIIE. The introduction of
n-alkyl groups induced thermal stability to the assemblies without affectingthe morphology of the peptide aggregates.