Self-Assembly Peptide Nanostructures

A special issue of Applied Sciences (ISSN 2076-3417). This special issue belongs to the section "Nanotechnology and Applied Nanosciences".

Deadline for manuscript submissions: closed (31 July 2018) | Viewed by 3020

Special Issue Editor


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Guest Editor
PEPSA-LAB, Department of Chemical Science and Technologies, University of Rome, Tor Vergata, 00133 Rome, Italy
Interests: peptide and protein nanotechnology; peptide materials; spectroscopy of biomolecules; peptide self-assembly; porphyrin aggregation and nanostructures
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Special Issue Information

Dear Colleagues,

In the last few years, peptide nanostructures have seen an explosion of interest, caused by extensive application in biomedicine (tissue engineering, antimicrobial activity, therapeutic peptides and vaccines, peptide-assisted drug delivery) and in bio-inspired nanotechnology (peptide-inorganic hybrids, peptide nanoparticles, peptide quantum dots). On the fundamental side, remarkable advancement of the knowledge of the mechanisms governing peptide self-assembly for generating nanostructures of different morphology (self-assembled monolayers, nanotubes, fibrils, nanowires) has also been achieved.

The control of the morphology of peptide aggregates at the nano- and mesoscale is crucial for application, linking complexity to function. In this connection, hierarchical self-assembly (i.e. the spontaneous association of molecular building blocks that achieves a different level of structural organization at each aggregation step) represents the most suitable approach for obtaining supramolecular architectures of specific shape and dimension.

This Special Issue aims to highlight the state-of-art of the research activity on the design and utilization of peptide nanostructures, gathering a collection of distinctive reviews and research articles concerning both fundamental and applicative aspects of the field.

I am confident that this publication will be of interest not only for the restricted community of peptide scientists, but it will intercept the attention of the broader interdisciplinary audience working on biomedicine and bionanotechnology.

Prof. Dr. Mariano Venanzi
Guest Editor

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Keywords

  • biomedicine

  • bionanotechnology

  • hierarchical self-assembly

  • peptide aggregation

  • peptide materials

  • peptide nanostructures

  • peptide self-assembly

Published Papers (1 paper)

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Research

15 pages, 5083 KiB  
Article
Electrochemical-QCMD Control over S-Layer (SbpA) Recrystallization with Fe2+ as Specific Ion for Self-Assembly Induction
by Jagoba Iturri, Andreas Breitwieser, Dietmar Pum, Uwe B. Sleytr and José Luis Toca-Herrera
Appl. Sci. 2018, 8(9), 1460; https://doi.org/10.3390/app8091460 - 25 Aug 2018
Cited by 1 | Viewed by 2688
Abstract
The critical role of divalent ions (M²+) in the self-assembly of SbpA S-layer proteins (from Lysinibacillus sphaericus CCM 2177) into crystalline structures has been reported in several studies. Hence, ions such as magnesium, barium, nickel and, most commonly, calcium (Ca²+ [...] Read more.
The critical role of divalent ions (M²+) in the self-assembly of SbpA S-layer proteins (from Lysinibacillus sphaericus CCM 2177) into crystalline structures has been reported in several studies. Hence, ions such as magnesium, barium, nickel and, most commonly, calcium (Ca²+) have proven to trigger both protein-protein and protein-substrate interactions involved in the two-stage non-classical pathway recrystallization followed by SbpA units. As a result, two dimensional, crystalline nanometric sheets in a highly ordered tetrameric state (p4) can be formed on top of different surfaces. The use of iron in its ferrous state (Fe2+) as self-assembly inducing candidate has been omitted so far due to its instability under aerobic conditions, tending to natural oxidation to the ferric (Fe3+) state. In this work, the potentiality of assembling fully functional S-layers from iron (II) salts (FeCl2 and FeSO4) is described for the first time. A combination of chemical (oxidation retardants) and electrical (−1 V potential) factors has been applied to effectively act against such an oxidizing trend. Formation of the respective crystalline films has been followed by means of Electrochemical Quartz Crystal Microbalance with Dissipation (EQCM-D) measurements and complementary Atomic Force Microscopy (AFM) topography studies, which prove the presence of squared lattice symmetry at the end of the recrystallization process. Both techniques, together with additional electrochemical tests performed over the ion permeability of both types of S-layer coatings formed, show the influence of the counterion chosen (chloride vs. sulphate) in the final packing and performance of the S-layer. The presence of an underlying Secondary Cell Wall Polymer (SCWP) as in the natural case contributes to pair both systems, due to the high lateral motility freedom provided by this biopolymer to SbpA units in comparison to uncoated substrates. Full article
(This article belongs to the Special Issue Self-Assembly Peptide Nanostructures)
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