Amphipathic peptides are attractive building blocks for the preparation of self-assembling, bio-inspired, and stimuli responsive nanomaterials with pharmaceutical interest. The bioavailability of these materials can be improved with the insertion of d amino acid residues to avoid fast proteolysis in vivo. With this knowledge, a new lauroyl peptide consisting of a sequence of glycine, glycine, d-serine, and d-lysine was designed. In spite of its simple sequence, this lipopeptide self-assembles into spherical micelles at acid pH, when the peptide moiety adopts disordered conformations. Self-aggregates reshape toward fibers at basic pH, following the conformational transition of the peptide region from random coil to β-sheet. Finally, hydrogels are achieved at basic pH and higher concentrations. The transition from random coil to β-sheet conformation of the peptide headgroup obtained by increasing pH was monitored by circular dichroism and vibrational spectroscopy. A structural analysis, performed by combining dynamic light scattering, small-angle X-ray scattering, transmission electron microscopy, and molecular dynamic simulations, demonstrated that the transition allows the self-assemblies to remodel from spherical micelles to rodlike shapes, to long fibers with rectangular cross-section and a head-tail-tail-head structure. The viscoelastic behavior of the hydrogels formed at the highest pH was investigated by rheology measurements.

Polymorphic self-organization of Lauroyl peptide in response to pH and concentration / Novelli, Federica; Strofaldi, Alessandro; De Santis, Serena; Del Giudice, Alessandra; Casciardi, Stefano; Galantini, Luciano; Morosetti, Stefano; Pavel, Nicolae Viorel; Masci, Giancarlo; Scipioni, Anita. - In: LANGMUIR. - ISSN 0743-7463. - 36:14(2020), pp. 3941-3951. [10.1021/acs.langmuir.9b02924]

Polymorphic self-organization of Lauroyl peptide in response to pH and concentration

Novelli, Federica;De Santis, Serena
Membro del Collaboration Group
;
Del Giudice, Alessandra
Membro del Collaboration Group
;
Galantini, Luciano
Membro del Collaboration Group
;
Morosetti, Stefano
Membro del Collaboration Group
;
Pavel, Nicolae Viorel
Membro del Collaboration Group
;
Masci, Giancarlo
Membro del Collaboration Group
;
Scipioni, Anita
Membro del Collaboration Group
2020

Abstract

Amphipathic peptides are attractive building blocks for the preparation of self-assembling, bio-inspired, and stimuli responsive nanomaterials with pharmaceutical interest. The bioavailability of these materials can be improved with the insertion of d amino acid residues to avoid fast proteolysis in vivo. With this knowledge, a new lauroyl peptide consisting of a sequence of glycine, glycine, d-serine, and d-lysine was designed. In spite of its simple sequence, this lipopeptide self-assembles into spherical micelles at acid pH, when the peptide moiety adopts disordered conformations. Self-aggregates reshape toward fibers at basic pH, following the conformational transition of the peptide region from random coil to β-sheet. Finally, hydrogels are achieved at basic pH and higher concentrations. The transition from random coil to β-sheet conformation of the peptide headgroup obtained by increasing pH was monitored by circular dichroism and vibrational spectroscopy. A structural analysis, performed by combining dynamic light scattering, small-angle X-ray scattering, transmission electron microscopy, and molecular dynamic simulations, demonstrated that the transition allows the self-assemblies to remodel from spherical micelles to rodlike shapes, to long fibers with rectangular cross-section and a head-tail-tail-head structure. The viscoelastic behavior of the hydrogels formed at the highest pH was investigated by rheology measurements.
2020
lipopeptide; peptide amphiphile: beta-sheet conformation; pH-sensitive peptide conformation; core-shell morphology; pH-sensitive morphology; sol-gel transition; hydrogel
01 Pubblicazione su rivista::01a Articolo in rivista
Polymorphic self-organization of Lauroyl peptide in response to pH and concentration / Novelli, Federica; Strofaldi, Alessandro; De Santis, Serena; Del Giudice, Alessandra; Casciardi, Stefano; Galantini, Luciano; Morosetti, Stefano; Pavel, Nicolae Viorel; Masci, Giancarlo; Scipioni, Anita. - In: LANGMUIR. - ISSN 0743-7463. - 36:14(2020), pp. 3941-3951. [10.1021/acs.langmuir.9b02924]
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11573/1404096
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