Fibrillar Self-Assembly of a Chimeric Elastin-Resilin Inspired Engineered Polypeptide

Bracalello, Angelo; Secchi, Valeria; Mastrantonio, Roberta; Pepe, Antonietta; Persichini, Tiziana; Iucci, Giovanna; Bochicchio, Brigida; Battocchio, Chiara

doi:10.3390/nano9111613

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Fibrillar Self-Assembly of a Chimeric Elastin-Resilin Inspired Engineered Polypeptide

¹,

^2,*

²,

¹,

²,

^1,*

and

Chiara Battocchio

^2,*

Department of Sciences, University of Basilicata, Via Ateneo Lucano, 10, 85100 Potenza, Italy

Department of Sciences, University of Roma Tre, Via della Vasca Navale, 79, 00146 Rome, Italy

Authors to whom correspondence should be addressed.

Nanomaterials 2019, 9(11), 1613; https://doi.org/10.3390/nano9111613

Received: 2 October 2019 / Revised: 1 November 2019 / Accepted: 11 November 2019 / Published: 14 November 2019

(This article belongs to the Special Issue Advanced Biocompatible Nanomaterials)

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Abstract

In the field of tissue engineering, recombinant protein-based biomaterials made up of block polypeptides with tunable properties arising from the functionalities of the individual domains are appealing candidates for the construction of medical devices. In this work, we focused our attention on the preparation and structural characterization of nanofibers from a chimeric-polypeptide-containing resilin and elastin domain, designed on purpose to enhance its cell-binding ability by introducing a specific fibronectin-derived Arg-Gly-Asp (RGD) sequence. The polypeptide ability to self-assemble was investigated. The molecular and supramolecular structure was characterized by Scanning Electronic Microscopy (SEM) and Atomic Force Microscopy (AFM), circular dichroism, state-of-the-art synchrotron radiation-induced techniques X-ray photoelectron spectroscopy (XPS) and near-edge X-ray absorption fine structure spectroscopy (NEXAFS). The attained complementary results allow us to assess as H-bonds influence the morphology of the aggregates obtained after the self-assembling of the chimeric polypeptide. Finally, a preliminary investigation of the potential cytotoxicity of the polypeptide was performed by culturing human fetal foreskin fibroblast (HFFF2) for its use as biomedical device. View Full-Text

Keywords: elastin; resilin; nanofibers; circular dichroism; cytotoxicity; self-assembly

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MDPI and ACS Style

Bracalello, A.; Secchi, V.; Mastrantonio, R.; Pepe, A.; Persichini, T.; Iucci, G.; Bochicchio, B.; Battocchio, C. Fibrillar Self-Assembly of a Chimeric Elastin-Resilin Inspired Engineered Polypeptide. Nanomaterials 2019, 9, 1613. https://doi.org/10.3390/nano9111613

AMA Style

Bracalello A, Secchi V, Mastrantonio R, Pepe A, Persichini T, Iucci G, Bochicchio B, Battocchio C. Fibrillar Self-Assembly of a Chimeric Elastin-Resilin Inspired Engineered Polypeptide. Nanomaterials. 2019; 9(11):1613. https://doi.org/10.3390/nano9111613

Chicago/Turabian Style

Bracalello, Angelo, Valeria Secchi, Roberta Mastrantonio, Antonietta Pepe, Tiziana Persichini, Giovanna Iucci, Brigida Bochicchio, and Chiara Battocchio. 2019. "Fibrillar Self-Assembly of a Chimeric Elastin-Resilin Inspired Engineered Polypeptide" Nanomaterials 9, no. 11: 1613. https://doi.org/10.3390/nano9111613

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Fibrillar Self-Assembly of a Chimeric Elastin-Resilin Inspired Engineered Polypeptide

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