Abstract
In summary, a change in the configuration of a single amino acid in a β3-heptapeptide can lead to remarkable changes in the physicochemical properties of the peptide with respect to the interaction with a (protein-free) biomimetic environment. Thus, the presence of an unnatural amino acid configuration in a peptide can have consequences not only with respect to specific interactions with proteins, but also, indirectly, with respect to the interaction with membrane lipids.
| Original language | English |
|---|---|
| Pages (from-to) | 1978-1981 |
| Number of pages | 4 |
| Journal | ChemBioChem |
| Volume | 10 |
| Issue number | 12 |
| DOIs | |
| Publication status | Published - Aug 17 2009 |
| Externally published | Yes |
Keywords
- Liposomes
- Peptides
- Phospholipids
- Structure-property relationships
- Vesicles
ASJC Scopus subject areas
- Biochemistry
- Molecular Medicine
- Molecular Biology
- Organic Chemistry
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Cite this
Shimanouchi, T., Walde, P., Gardiner, J., Capone, S., Seebach, D., & Kuboi, R. (2009). Inversion of the configuration of a single stereocenter in a β-heptapeptide leads to drastic changes in its interaction with phospholipid bilayers. ChemBioChem, 10(12), 1978-1981. https://doi.org/10.1002/cbic.200900175