Stabilization of Peptide Fibrils by Hydrophobic Interaction
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- 作者：Joris T. Meijer ; Marjolijn Roeters ; Valentina Viola ; Dennis W. P. M. Lö ; wik ; Gert Vriend ; Jan C. M. van Hest
- 刊名：Langmuir
- 出版年：2007
- 出版时间：February 13, 2007
- 年：2007
- 卷：23
- 期：4
- 页码：2058 - 2063
- 全文大小：405K
- 年卷期：v.23,no.4(February 13, 2007)
- ISSN：1520-5827
文摘
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 
-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.
-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.