Abstract

Over the years, a large number of multidisciplinary investigations has unveiled that the self-assembly of short peptides and even of individual amino acids can generate a variety of different biomaterials. In this framework, we have recently reported that polyethylene glycol (PEG) conjugates of short homopeptides, containing aromatic amino acids such as phenylalanine (Phe, F) and naphthylalanine (Nal), are able to form elongated fibrillary aggregates having interesting chemical and physical properties. We here extend these analyses characterizing the self-assembling propensity of PEG(6)-W4, a PEG adduct of the tetra-tryptophan (W4) sequence. A comprehensive structural characterization of PEG(6)-W4 was obtained, both in solution and at the solid state, through the combination of spectroscopic, microscopic, X-ray scattering and computational techniques. Collectively, these studies demonstrate that this peptide is able to self-assemble in fibrillary networks characterized by a cross -structure spine. The present findings clearly demonstrate that aromatic residues display a general propensity to induce self-aggregation phenomenon, despite the significant differences in the physicochemical properties of their side chains.

Autore Pugliese

• Giannini Cinzia , Sibillano Teresa

Tutti gli autori

• Diaferia C.; Balasco N.; Sibillano T.; Giannini C.; Vitagliano L.; Morelli G.C.; Accardo A.

Titolo volume/Rivista

ChemPhysChem

Anno di pubblicazione

2018

ISSN

1439-4235

ISBN

Non Disponibile

Numero di citazioni Wos

Nessuna citazione

Ultimo Aggiornamento Citazioni

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Numero di citazioni Scopus

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Ultimo Aggiornamento Citazioni

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Settori ERC

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Codici ASJC

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