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

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 C(16)-βAH, contains a dipeptide headgroup corresponding to the bioa...

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Veröffentlicht in:Langmuir : the ACS journal of surfaces and colloids. - 1985. - 28(2012), 31 vom: 07. Aug., Seite 11599-608
1. Verfasser: Castelletto, V (VerfasserIn)
Weitere Verfasser: Cheng, G, Stain, C, Connon, C J, Hamley, I W
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2012
Zugriff auf das übergeordnete Werk:Langmuir : the ACS journal of surfaces and colloids
Schlagworte:Journal Article Research Support, Non-U.S. Gov't Biocompatible Materials Dipeptides Lipid Bilayers Surface-Active Agents Unilamellar Liposomes hexadecyl-(beta-alaninehistidine) Water 059QF0KO0R mehr... 1,2-Dipalmitoylphosphatidylcholine 2644-64-6 Carnosine 8HO6PVN24W
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520 |a 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 C(16)-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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650 4 |a Research Support, Non-U.S. Gov't 
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650 7 |a Dipeptides  |2 NLM 
650 7 |a Lipid Bilayers  |2 NLM 
650 7 |a Surface-Active Agents  |2 NLM 
650 7 |a Unilamellar Liposomes  |2 NLM 
650 7 |a hexadecyl-(beta-alaninehistidine)  |2 NLM 
650 7 |a Water  |2 NLM 
650 7 |a 059QF0KO0R  |2 NLM 
650 7 |a 1,2-Dipalmitoylphosphatidylcholine  |2 NLM 
650 7 |a 2644-64-6  |2 NLM 
650 7 |a Carnosine  |2 NLM 
650 7 |a 8HO6PVN24W  |2 NLM 
700 1 |a Cheng, G  |e verfasserin  |4 aut 
700 1 |a Stain, C  |e verfasserin  |4 aut 
700 1 |a Connon, C J  |e verfasserin  |4 aut 
700 1 |a Hamley, I W  |e verfasserin  |4 aut 
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