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Self-Assembly of a Peptide Amphiphile Containing l-Carnosine and Its Mixtures with a Multilamellar Vesicle Forming Lipid

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† School of Chemistry, Food Science and Pharmacy, University of Reading, Whiteknights, Reading RG6 6AD, United Kingdom
‡ Centre for Advanced Microscopy, University of Reading, Whiteknights, Reading RG6 6AF, United Kingdom
*E-mail: [email protected]; [email protected]
Cite this: Langmuir 2012, 28, 31, 11599–11608
Publication Date (Web):July 12, 2012
https://doi.org/10.1021/la302210b
Copyright © 2012 American Chemical Society
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Abstract

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The self-assembly of the peptide amphiphile (PA) hexadecyl-(β-alanine-histidine) is examined in aqueous solution, along with its mixtures with multilamellar vesicles formed by DPPC (dipalmitoyl phosphatidylcholine). This PA, denoted C16-βAH, contains a dipeptide headgroup corresponding to the bioactive molecule l-carnosine. It is found to self-assemble into nanotapes based on stacked layers of molecules. Bilayers are found to coexist with monolayers in which the PA molecules pack with alternating up–down arrangement so that the headgroups decorate both surfaces. The bilayers become dehydrated as PA concentration increases and the number of layers in the stack decreases to produce ultrathin nanotapes comprised of 2–3 bilayers. Addition of the PA to DPPC multilamellar vesicles leads to a transition to well-defined unilamellar vesicles. The unique ability to modulate the stacking of this PA as a function of concentration, combined with its ability to induce a multilamellar to unilamellar thinning of DPPC vesicles, may be useful in biomaterials applications where the presentation of the peptide function at the surface of self-assembled nanostructures is crucial.

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Scheme illustrating representative C16-βAH samples. CD, POM, cryo-SEM, and FTIR data for C16-βAH; FTIR data for DPPC solution and DPPC/C16-βAH mixtures. This material is available free of charge via the Internet at http://pubs.acs.org.

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