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Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides
Published on: November 21, 2013
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Self-assembly of three bacterially-derived bioactive lipopeptides
Ian W Hamley1, Ashkan Dehsorkhi, Paula Jauregi
1School of Chemistry, Pharmacy and Food Biosciences, University of Reading, Whiteknights, Reading, RG6 6AD, UK.
Soft Matter
|June 2, 2015
Summary
Bacillus subtilis lipopeptides surfactin, plipastatin, and mycosubtilin self-assemble differently in water. Mycosubtilin forms nanotapes, unlike the spherical micelles of surfactin and plipastatin, due to its unique headgroup and chain structure.
Area of Science:
- Biochemistry
- Materials Science
- Microbiology
Background:
- Lipopeptides from Bacillus subtilis are amphiphilic molecules with potential applications.
- Understanding their self-assembly behavior is crucial for controlling material properties.
Purpose of the Study:
- To investigate and compare the aqueous self-assembly of three distinct Bacillus subtilis lipopeptides: surfactin, plipastatin, and mycosubtilin.
- To elucidate the structural basis for differing self-assembly mechanisms.
Main Methods:
- Cryogenic transmission electron microscopy (cryo-TEM)
- X-ray scattering
- Circular dichroism (CD) spectroscopy
- Fourier-transform infrared (FTIR) spectroscopy
Main Results:
- Surfactin and plipastatin self-assembled into spherical micelles with a 2 nm radius.
- Mycosubtilin exhibited a contrasting self-assembly, forming extended nanotapes via bilayer ordering.
- CD and FTIR spectroscopy confirmed turn structures in the cyclic peptide headgroups.
Conclusions:
- The distinct self-assembly of mycosubtilin is attributed to its unique surfactant packing parameter.
- Specific features of mycosubtilin's peptide headgroup conformation and alkyl chain branching drive its divergent assembly into nanotapes.
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