The preparation and self-assembly of short hydrophobic peptides able to solubilize in water through the formation of supramolecular assembly is reported. The two diastereoisomeric pentapeptides AcAla-NRB-Ala-Aib-AlaNH21 and 2 containing the two enantiomers of non-proteinogenic norbornene amino acid (NRB) were synthesized in an efficient way and in good yields. They were insoluble in organic solvent, except MeOH and DMSO, but completely soluble in water despite that they are made of hydrophobic amino acids. The formation of a supramolecular assembly in water was assessed by Transmission Electron Microscopy (TEM) and Dynamic Light Scattering (DLS) using 1 and 2 individually or in a mixture. Conformational analysis on the two diastereoisomers, performed in CD3CN, CD3OH and in H2O/D2O, indicated the formation of a stable 310-helix structure for both peptides: the helix structure is more stable in CD3CN and CD3OH than in H2O/D2O where a helix/random coil transition was observed. Apparently, the norbornene moiety plays a role in the stabilization, in fact 1R2R3R-norbornene AA present in peptide 2 induces a more stable secondary structure with respect to the 1S2S3S-isomer present in peptide 1.

Aqueous self-assembly of short hydrophobic peptides containing norbornene amino acid into supramolecular structures with spherical shape / A. Ruffoni, M.V. Cavanna, S. Argentiere, S. Locarno, S. Pellegrino, M.L. Gelmi, F. Clerici. - In: RSC ADVANCES. - ISSN 2046-2069. - 6:93(2016), pp. 90754-90759.

Aqueous self-assembly of short hydrophobic peptides containing norbornene amino acid into supramolecular structures with spherical shape

A. Ruffoni
Primo
;
S. Locarno;S. Pellegrino;M.L. Gelmi
Penultimo
;
F. Clerici
Ultimo
2016

Abstract

The preparation and self-assembly of short hydrophobic peptides able to solubilize in water through the formation of supramolecular assembly is reported. The two diastereoisomeric pentapeptides AcAla-NRB-Ala-Aib-AlaNH21 and 2 containing the two enantiomers of non-proteinogenic norbornene amino acid (NRB) were synthesized in an efficient way and in good yields. They were insoluble in organic solvent, except MeOH and DMSO, but completely soluble in water despite that they are made of hydrophobic amino acids. The formation of a supramolecular assembly in water was assessed by Transmission Electron Microscopy (TEM) and Dynamic Light Scattering (DLS) using 1 and 2 individually or in a mixture. Conformational analysis on the two diastereoisomers, performed in CD3CN, CD3OH and in H2O/D2O, indicated the formation of a stable 310-helix structure for both peptides: the helix structure is more stable in CD3CN and CD3OH than in H2O/D2O where a helix/random coil transition was observed. Apparently, the norbornene moiety plays a role in the stabilization, in fact 1R2R3R-norbornene AA present in peptide 2 induces a more stable secondary structure with respect to the 1S2S3S-isomer present in peptide 1.
chemistry (all); chemical engineering (all)
Settore CHIM/06 - Chimica Organica
Sintesi e applicazioni biomediche di peptidomimetici in campo oncologico
Article (author)
File in questo prodotto:
File Dimensione Formato  
Ruffoni_C6RA17116H.pdf

accesso aperto

Tipologia: Publisher's version/PDF
Dimensione 872.22 kB
Formato Adobe PDF
872.22 kB Adobe PDF Visualizza/Apri
Pubblicazioni consigliate

Caricamento pubblicazioni consigliate

I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.

Utilizza questo identificativo per citare o creare un link a questo documento: http://hdl.handle.net/2434/444834
Citazioni
  • ???jsp.display-item.citation.pmc??? ND
  • Scopus 11
  • ???jsp.display-item.citation.isi??? 10
social impact