Abstract

The ability of peptides to self-assemble represents a valuable tool for the development of biomaterialsof biotechnological and/or biomedical interest. Diphenylalanine homodimer (FF) and its analogues areamong the most promising systems in this field. The longest Phe-based building block hithertocharacterized is pentaphenylalanine (F5). We studied the aggregation propensity and the structural/morphological features of assemblies of zwitterionic hexaphenylalanine H+-F6-O and of three variantscharacterized by different charged states of the terminal ends (Ac-F6-Amide, H+-F6-Amide and Ac-F6-O).As previously observed for PEGylated hexaphenylalanine (PEG8-F6), all F6 variants show a strong tendencyto form b-rich assemblies in which the structural motif is constituted by antiparallel b-strands in thecross-b framework. Extensive replica exchange molecular dynamics simulations carried out on a pairs ofF6 peptides indicate that the antiparallel b-structure of the final assemblies is likely dictated by thepreferred association modes of the individual chains in the very early stages of the aggregation process.Our data suggest that even very small F6 peptides are properly pre-organized and prone to the build-upof the final assembly.

Autore Pugliese

• Giannini Cinzia , Altamura Davide , Sibillano Teresa

Tutti gli autori

• Diaferia C.; Balasco N.; Altamura D.; Sibillano T.; Gallo E. ; Roviello V.; Giannini C.; Morelli G.C.; Vitagliano L.; Accardo A.

Titolo volume/Rivista

Soft matter

Anno di pubblicazione

2018

ISSN

1744-683X

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

Non Disponibile