Stabilization of peptide fibrils by hydrophobic interaction.
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.
Meijer
Joris T
JT
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.
Roeters
Marjolijn
M
Viola
Valentina
V
Löwik
Dennis W P M
DW
Vriend
Gert
G
van Hest
Jan C M
JC
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
D010455:Peptides