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Analytical and Bioanalytical Chemistry

, Volume 410, Issue 20, pp 4925–4941 | Cite as

Interactions between elastin-like peptides and an insulating poly(ortho-aminophenol) membrane investigated by AFM and XPS

  • Maria Elvira CarboneEmail author
  • Rosanna Ciriello
  • Pasquale Moscarelli
  • Federica Boraldi
  • Giuliana Bianco
  • Antonio Guerrieri
  • Brigida Bochicchio
  • Antonietta Pepe
  • Daniela Quaglino
  • Anna Maria SalviEmail author
Research Paper

Abstract

This investigation was undertaken to explore the mutual recognition of the pentapeptide (ValGlyGlyValGly)n, a hydrophobic elastin-like peptide (ELP), suspended in deionized water in monomer (n = 1) and trimer (n = 3) forms and the outer surface of a very thin, insulating polymer, poly(ortho-aminophenol) (PoAP), electrochemically grown on a platinum foil by cyclic voltammetry in a neutral medium (phosphate-buffered saline, I = 0.1M) immersed in the suspension. As a prior task, the proved propensity of the ValGlyGlyValGly sequence, at the given minimal length (three or more repeats), to self-assemble into amyloid-like fibrils when solubilized in an aqueous environment was considered within the framework of testing PoAP surfaces for the specific detection of amyloid precursors. From our knowledge of the chemical structure and physical properties of both biomacromolecule families obtained in previous studies, we focused on the efficacy of the binding sites offered to ELP fibrils by PoAP in its as-prepared form or properly modified either by postsynthesis oxidation or by adsorption/entrapping of ELP monomer(s) with or without protecting terminal groups. Consistent with all methods of preparation, the best surfaces, recognizable by the trimer fibrils, are those modified to carry a larger number of carbonyls, particularly by entrapment of ELP monomer(s) during PoAP electrosynthesis using an imprinting-inspired method. The degree of attachment of fibrillar aggregates, detected by atomic force microscopy and X-ray photoelectron spectroscopy, provides unequivocal evidence of the cooperative forces involving PoAP–ELP interactions. The results obtained suggest the prospect of using the proposed Pt/PoAP/ELP systems as biodetectors in Alzheimer disease.

Graphical abstract

Synthesis steps of Pt/PoAP/ELP electrodes for amyloid detection. AFM = Atomic Force Microscopy, CV = Cyclic Voltammetry, ELPs = Elastin like Peptides, PoAP = Poly ortho-Aminophenol, Pt = Platinum, XPS = X-ray Photoelectron Spectroscopy

Keywords

X-ray photoelectron spectroscopy Atomic force microscopy Poly(ortho-aminophenol) Elastin-like peptides Amyloids Peptide-imprinted cyclic voltammetry polymerization 

Notes

Acknowledgements

The authors are grateful to Fausto Langerame for acquisition of X-ray photoelectron spectra and technical assistance. The Surface Microscopy Laboratory of the Science Department (University of Basilicata) is acknowledged for the use of electrochemical and atomic force microscopy instrumentation during the PhD studies of MEC (A.Y. 2015-2016).

Compliance with ethical standards

Conflict of interest

The authors declare that they have no competing interests.

Supplementary material

216_2018_1142_MOESM1_ESM.pdf (788 kb)
ESM 1 (PDF 788 kb)

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Copyright information

© Springer-Verlag GmbH Germany, part of Springer Nature 2018

Authors and Affiliations

  • Maria Elvira Carbone
    • 1
    Email author
  • Rosanna Ciriello
    • 1
  • Pasquale Moscarelli
    • 2
  • Federica Boraldi
    • 2
  • Giuliana Bianco
    • 1
  • Antonio Guerrieri
    • 1
  • Brigida Bochicchio
    • 1
  • Antonietta Pepe
    • 1
  • Daniela Quaglino
    • 2
  • Anna Maria Salvi
    • 1
    Email author
  1. 1.Dipartimento di ScienzeUniversità degli Studi della BasilicataPotenzaItaly
  2. 2.Dipartimento di Scienze della VitaUniversità degli Studi di Modena e Reggio EmiliaModenaItaly

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