Tuning secondary structure and self-assembly of amphiphilic peptides

Self-assembly is one of nature's mechanisms by which higher order structures are obtained. Two of the main driving forces for self-assembly, hydrophobic interactions and hydrogen bonding, are both present within amphiphilic peptides. Here, it is demonstrated how the intricately interconnected f...

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Veröffentlicht in:Langmuir Jg. 21; H. 2; S. 524
Hauptverfasser: Löwik, Dennis W P M, Garcia-Hartjes, Jaime, Meijer, Joris T, van Hest, Jan C M
Format: Journal Article
Sprache:Englisch
Veröffentlicht: United States 18.01.2005
Schlagworte:
Acylation
Amino Acid Sequence
Circular Dichroism
Microscopy, Electron
Molecular Sequence Data
Molecular Structure
Peptides - chemistry
Protein Structure, Secondary
Surface-Active Agents - chemistry
ISSN:0743-7463
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Zusammenfassung:Self-assembly is one of nature's mechanisms by which higher order structures are obtained. Two of the main driving forces for self-assembly, hydrophobic interactions and hydrogen bonding, are both present within amphiphilic peptides. Here, it is demonstrated how the intricately interconnected folding and assembly behavior of an N-terminally acylated peptide, with the sequence GANPNAAG, has been tuned by varying its hydrophobic tail and thermal history. The change in interplay between hydrophobic forces and peptide folding allowed the occurrence of different types of aggregation, from soluble peptides with a random coil conformation to aggregated peptides arranged in a beta-sheet assembly, which form helically twisted bilayer ribbons.
Bibliographie:ObjectType-Article-2
SourceType-Scholarly Journals-1
ObjectType-Correspondence-1
content type line 23
ISSN:0743-7463
DOI:10.1021/la047578x