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Thermally regulated reversible formation of vesicle-like assemblies by hexaproline amphiphiles

Felip-León, C., Galindo, F., Miravet, J. F., Castelletto, V. and Hamley, I. W. ORCID: (2017) Thermally regulated reversible formation of vesicle-like assemblies by hexaproline amphiphiles. The Journal of Physical Chemistry B, 121 (31). pp. 7443-7446. ISSN 1520-6106

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To link to this item DOI: 10.1021/acs.jpcb.7b06167


Peptides composed of hexaproline and glutamic acid (P6E) or lysine (P6K) as C-terminal units show thermally promoted aggregation, affording vesicle-like assemblies upon heating to 80 ºC. The aggregation is analyzed by dynamic light scattering (DLS), with number averaged diameters of ca. 600 and 300 nm respectively for P6E and P6K. NMR studies reveal that upon heating the amount of NMR-visible species is reduced to ca. 50% and that an important conformational change is experienced by the molecules in solution. Circular dichroism (CD) shows that at 20º C the peptides present a polyproline II (PP-II) conformation which is disorganized upon heating. Scanning electron microscopy for samples which were fast frozen at 80 ºC reveals vesicle-like assemblies. Using pyrene as a fluorescence probe, a critical aggregation concentration of ca. 30 m was estimated for P6E while that of P6K was above 0.6 mM. The aggregation process is found to be fully reversible and could serve as a basis for development of stimuli responsive carriers.

Item Type:Article
Divisions:Life Sciences > School of Chemistry, Food and Pharmacy > Department of Chemistry
ID Code:71457


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