Polymorphic self-organization of Lauroyl peptide in response to pH and concentration
| Autor: | Luciano Galantini, Stefano Casciardi, Nicolae Viorel Pavel, Alessandra Del Giudice, Serena De Santis, Stefano Morosetti, Giancarlo Masci, Alessandro Strofaldi, Anita Scipioni, Federica Novelli |
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| Přispěvatelé: | Novelli, Federica, Strofaldi, Alessandro, De Santis, Serena, Del Giudice, Alessandra, Casciardi, Stefano, Galantini, Luciano, Morosetti, Stefano, Pavel, Nicolae Viorel, Masci, Giancarlo, Scipioni, Anita |
| Jazyk: | angličtina |
| Rok vydání: | 2020 |
| Předmět: |
Circular dichroism
Peptide 02 engineering and technology 010402 general chemistry 01 natural sciences Micelle Molecular dynamics pH-sensitive morphology Dynamic light scattering Amphiphile Electrochemistry General Materials Science peptide amphiphile: beta-sheet conformation Amino Acids Spectroscopy chemistry.chemical_classification core-shell morphology Chemistry Circular Dichroism Hydrogels Surfaces and Interfaces Hydrogen-Ion Concentration 021001 nanoscience & nanotechnology Condensed Matter Physics Random coil 0104 chemical sciences Crystallography pH-sensitive peptide conformation lipopeptide Self-healing hydrogels sol-gel transition hydrogel Peptides 0210 nano-technology |
| Popis: | Amphipathic peptides are attractive building blocks for the preparation of self-assembling, bio-inspired and stimuli responsive nano-materials 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. The self-aggregates reshape towards 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 rod-like 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. |
| Databáze: | OpenAIRE |
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