Stabilization of peptide fibrils by hydrophobic interaction
| Autor: | Gert Vriend, Joris T. Meijer, Marjolijn Roeters, Dennis W. P. M. Löwik, Valentina Viola, Jan C. M. van Hest |
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| Rok vydání: | 2007 |
| Předmět: |
Chemical and physical biology [NCMLS 7]
Bioinformatics Stereochemistry Peptide Sequence (biology) Fibril Bio-Organic Chemistry Hydrophobic effect Microscopy Electron Transmission Amphiphile Electrochemistry General Materials Science Thermal stability Amino Acid Sequence Spectroscopy Alkyl chemistry.chemical_classification Hydrogen bond Circular Dichroism Temperature Surfaces and Interfaces Condensed Matter Physics chemistry Biophysics Peptides Cellular energy metabolism [UMCN 5.3] Hydrophobic and Hydrophilic Interactions |
| Zdroj: | Langmuir, 23, 2058-63 Langmuir, 23, 4, pp. 2058-63 |
| ISSN: | 0743-7463 |
| Popis: | Contains fulltext : 36489.pdf (Publisher’s version ) (Closed access) 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. |
| Databáze: | OpenAIRE |
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