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|e rakwb
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|a eng
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| 100 |
1 |
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|a Meijer, Joris T
|e verfasserin
|4 aut
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| 245 |
1 |
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|a Stabilization of peptide fibrils by hydrophobic interaction
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| 264 |
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|c 2007
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| 336 |
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|a Text
|b txt
|2 rdacontent
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| 337 |
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|a ohne Hilfsmittel zu benutzen
|b n
|2 rdamedia
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| 338 |
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|a Band
|b nc
|2 rdacarrier
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|a Date Completed 02.05.2007
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|a Date Revised 18.11.2010
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|a published: Print
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|a Citation Status MEDLINE
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| 520 |
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|a 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
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|a Journal Article
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| 650 |
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7 |
|a Peptides
|2 NLM
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| 700 |
1 |
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|a Roeters, Marjolijn
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Viola, Valentina
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Löwik, Dennis W P M
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Vriend, Gert
|e verfasserin
|4 aut
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| 700 |
1 |
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|a van Hest, Jan C M
|e verfasserin
|4 aut
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| 773 |
0 |
8 |
|i Enthalten in
|t Langmuir : the ACS journal of surfaces and colloids
|d 1992
|g 23(2007), 4 vom: 13. Feb., Seite 2058-63
|w (DE-627)NLM098181009
|x 1520-5827
|7 nnns
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| 773 |
1 |
8 |
|g volume:23
|g year:2007
|g number:4
|g day:13
|g month:02
|g pages:2058-63
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|d 23
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|h 2058-63
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