Self-assembly of surfactant-like peptides.
Inspired by recent work describing surfactant-like peptides, we have carried out a systematic study on peptides with the underlying composition of V6D2, altering the absolute sequence to determine the importance of the surfactant-like structure. All of the peptides examined here formed self-assembled structures in water. However, in contrast to other reports, we have found a surprising diversity of structures including fibers, tapes, and twisted ribbons but an absence of the vesicles and nanotubes described previously. Further investigations demonstrated that peptide purity plays a significant role in the outcome of the self-assembly. Different batches behave very differently, which can be linked to the compositions of these batches. This work shows that there is a need for not only rational design but also ease of synthesis of the building blocks for self-assembled structures.
Adams
Dave J
DJ
Unilever Corporate Research, Colworth Science Park, Sharnbrook, Bedford, UK. dave.adams@unilever.com
Holtzmann
Kathrin
K
Schneider
Christian
C
Butler
Michael F
MF
D002851:Chromatography, High Pressure Liquid / Q000379:methods; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D010316:Particle Size; D010455:Peptides / Q000737:chemistry*; D013499:Surface Properties; D013501:Surface-Active Agents / Q000737:chemistry*; D014867:Water / Q000737:chemistry
D010455:Peptides; D013501:Surface-Active Agents; D014867:Water