Self-assembly of Fmoc-diphenylalanine inside liquid marbles

• Published in: Colloids and surfaces, B, Biointerfaces Vol. 97; pp. 43 - 50
• Main Authors: Braun, Hans-Georg, Cardoso, André Zamith
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 01.09.2012
• Subjects: acidification; air; aqueous solutions; colloids; Electron diffraction; Fluorenes - chemistry; Interface bottom-up design; interphase; Liquid marbles; Lycopodium; Lycopodium clavatum spores; Micro-to-nano hierarchical self-assembly; Microreactor; Nanoparticles - chemistry; Nanostructures - chemistry; Peptide gels; Phenylalanine - analogs & derivatives; Phenylalanine - chemistry; scanning electron microscopy; spores; Supramolecular biochemistry; Surface Properties; transmission electron microscopy; Lycopodium clavatum spores; Liquid marbles; Electron diffraction; Microreactor; Interface bottom-up design; Supramolecular biochemistry; Peptide gels; Micro-to-nano hierarchical self-assembly
• ISSN: 0927-7765; 1873-4367
• DOI: 10.1016/j.colsurfb.2012.03.028

[Display omitted] ► Self-assembly of peptide at the air/liquid interface. ► Stabilization of liquid marbles through peptide membranes. ► Electron diffraction data of self-assembled peptide membranes. Liquid marbles made from Lycopodium clavatum spores are used to encapsulate aqueous solutions of 9-fluorenylmethoxycarbonyl-diphenylalanine (Fmoc-FF). Acidification of the Fmoc-FF solution at the liquid/air interface of the liquid marble triggers the self-assembly of ribbon-like peptide fibrils into an ultrathin peptide membrane (50–500nm). The membrane incorporates the lycopodium microparticles and as a result stabilizes the liquid marble against collapse, that could otherwise occur through particle disintegration at the floating interphase. Ultrathin nanostructured peptide membrane formation at the liquid/air interface is also observed within artificial microstructured floating objects. Thus, peptide membranes formed were inspected by SEM and TEM. Electron diffraction data reveal information about the molecular organization inside the oligopeptide membranes.