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Self-assembly of a peptide amphiphile containing l-carnosine and its mixtures with a multilamellar vesicle forming lipid

Castelletto, V., Cheng, G., Stain, C., Connon, C. and Hamley, I. ORCID: (2012) Self-assembly of a peptide amphiphile containing l-carnosine and its mixtures with a multilamellar vesicle forming lipid. Langmuir, 28 (31). pp. 11599-11608. ISSN 0743-7463

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To link to this item DOI: 10.1021/la302210b


The self-assembly of the peptide amphiphile (PA) hexadecyl-(β-alaninehistidine) 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 selfassemble 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.

Item Type:Article
Divisions:Interdisciplinary centres and themes > Chemical Analysis Facility (CAF)
Life Sciences > School of Chemistry, Food and Pharmacy > Department of Chemistry
Interdisciplinary centres and themes > Chemical Analysis Facility (CAF) > Electron Microscopy Laboratory (CAF)
ID Code:28942
Publisher:American Chemical Society


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