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Bioinspired Peptide/Protein Nanomaterials: Form-Structure-Function
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Bioinspired Peptide/Protein Nanomaterials: Form-Structure-Function

A special issue of Molecules (ISSN 1420-3049). This special issue belongs to the section "Bioorganic Chemistry".

Deadline for manuscript submissions: closed (31 July 2021) | Viewed by 13720

Special Issue Editor

Dr. Scott H. Medina

E-Mail Website
Guest Editor
Department of Biomedical Engineering, Pennsylvania State University, State College, PA, USA
Interests: de novo peptide design; chemical biology; supramolecular chemistry; antimicrobial peptides; anticancer peptides; nanomedicine; microbiome engineering; drug delivery; gene delivery; biomacromolecule self-assembly

Special Issue Information

Dear Colleagues,

Nature’s ability to hierarchically assemble intricate nanoarchitectures has captivated and inspired biologists, chemists, physicists, and material scientists alike. Advances in our understanding of the complex interplay between nano-topography/morphology and physicochemical properties of biomacromolecular structures has given rise to bioresponsive materials and adaptive matter. For example, comprehensive structure–activity relationships of peptide/protein self-assembly have informed the design of thermodynamically and kinetically trapped supramolecular nanostructures that serve as the nucleus for “smart” nano-biotechnologies. Utilizing natural peptides and proteins as templates, de novo materials are now being designed to mimic nature, or in some cases engineered with non-natural functionalities, creating new opportunities in biomedicine, catalysis, photonics, and other fields.

This Special Issue on bioinspired peptide/protein nanomaterials seeks to advance our fundamental understanding of the synthesis, supramolecular self-assembly, and hierarchical structures of naturally occurring materials, and use this knowledge to engineer new bioinspired and adaptive nanomaterials for diverse applications. Original research articles, communications, and reviews covering novel approaches in the de novo design and fabrication of engineered biomimetic nanomaterials are welcome. Structure–activity relationships of bioinspired nanotechnologies, and the practical application of these systems in medicine, chemistry, and energy, are of special interest.

Dr. Scott H. Medina
Guest Editor

Manuscript Submission Information

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Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Molecules is an international peer-reviewed open access semimonthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2700 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • Biological and bio-inspired nano-structures
  • De novo peptide and protein design
  • Functional peptide/protein nanomaterials
  • Technological application of bioinspired self-assemblies
  • Hybrid peptide- and protein-based nanomaterials
  • Peptide/protein nanofibers and hydrogels
  • Hierarchically structured nanomaterials
  • Structure–property relationships

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Published Papers (4 papers)

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Research

15 pages, 19498 KiB  
Article
Computational Design of Single-Peptide Nanocages with Nanoparticle Templating
by José A. Villegas, Nairiti J. Sinha, Naozumi Teramoto, Christopher D. Von Bargen, Darrin J. Pochan and Jeffery G. Saven
Molecules 2022, 27(4), 1237; https://doi.org/10.3390/molecules27041237 - 12 Feb 2022
Cited by 6 | Viewed by 2844
Abstract
Protein complexes perform a diversity of functions in natural biological systems. While computational protein design has enabled the development of symmetric protein complexes with spherical shapes and hollow interiors, the individual subunits often comprise large proteins. Peptides have also been applied to self-assembly, [...] Read more.
Protein complexes perform a diversity of functions in natural biological systems. While computational protein design has enabled the development of symmetric protein complexes with spherical shapes and hollow interiors, the individual subunits often comprise large proteins. Peptides have also been applied to self-assembly, and it is of interest to explore such short sequences as building blocks of large, designed complexes. Coiled-coil peptides are promising subunits as they have a symmetric structure that can undergo further assembly. Here, an α-helical 29-residue peptide that forms a tetrameric coiled coil was computationally designed to assemble into a spherical cage that is approximately 9 nm in diameter and presents an interior cavity. The assembly comprises 48 copies of the designed peptide sequence. The design strategy allowed breaking the side chain conformational symmetry within the peptide dimer that formed the building block (asymmetric unit) of the cage. Dynamic light scattering (DLS) and transmission electron microscopy (TEM) techniques showed that one of the seven designed peptide candidates assembled into individual nanocages of the size and shape. The stability of assembled nanocages was found to be sensitive to the assembly pathway and final solution conditions (pH and ionic strength). The nanocages templated the growth of size-specific Au nanoparticles. The computational design serves to illustrate the possibility of designing target assemblies with pre-determined specific dimensions using short, modular coiled-coil forming peptide sequences. Full article
(This article belongs to the Special Issue Bioinspired Peptide/Protein Nanomaterials: Form-Structure-Function)
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12 pages, 2879 KiB  
Article
Formation of Microcages from a Collagen Mimetic Peptide via Metal-Ligand Interactions
by Jeremy Gleaton, Ryan W. Curtis and Jean Chmielewski
Molecules 2021, 26(16), 4888; https://doi.org/10.3390/molecules26164888 - 12 Aug 2021
Cited by 3 | Viewed by 2616
Abstract
Here, the hierarchical assembly of a collagen mimetic peptide (CMP) displaying four bipyridine moieties is described. The CMP was capable of forming triple helices followed by self-assembly into disks and domes. Treatment of these disks and domes with metal ions such as Fe(II), [...] Read more.
Here, the hierarchical assembly of a collagen mimetic peptide (CMP) displaying four bipyridine moieties is described. The CMP was capable of forming triple helices followed by self-assembly into disks and domes. Treatment of these disks and domes with metal ions such as Fe(II), Cu(II), Zn(II), Co(II), and Ru(III) triggered the formation of microcages, and micron-sized cup-like structures. Mechanistic studies suggest that the formation of the microcages proceeds from the disks and domes in a metal-dependent fashion. Fluorescently-labeled dextrans were encapsulated within the cages and displayed a time-dependent release using thermal conditions. Full article
(This article belongs to the Special Issue Bioinspired Peptide/Protein Nanomaterials: Form-Structure-Function)
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15 pages, 3021 KiB  
Article
Dopamine Self-Polymerization as a Simple and Powerful Tool to Modulate the Viscoelastic Mechanical Properties of Peptide-Based Gels
by Galit Fichman and Joel P. Schneider
Molecules 2021, 26(5), 1363; https://doi.org/10.3390/molecules26051363 - 4 Mar 2021
Cited by 16 | Viewed by 5124
Abstract
Dopamine is a small versatile molecule used for various biotechnological and biomedical applications. This neurotransmitter, in addition to its biological role, can undergo oxidative self-polymerization to yield polydopamine, a robust universal coating material. Herein, we harness dopamine self-polymerization to modulate the viscoelastic mechanical [...] Read more.
Dopamine is a small versatile molecule used for various biotechnological and biomedical applications. This neurotransmitter, in addition to its biological role, can undergo oxidative self-polymerization to yield polydopamine, a robust universal coating material. Herein, we harness dopamine self-polymerization to modulate the viscoelastic mechanical properties of peptide-based gels, expanding their ever-growing application potential. By combining rapid peptide assembly with slower dopamine auto-polymerization, a double network gel is formed, where the fibrillar peptide gel network serves as a scaffold for polydopamine deposition, allowing polydopamine to interpenetrate the gel network as well as establishing crosslinks within the matrix. We have shown that triggering the assembly of a lysine-rich peptide gelator in the presence of dopamine can increase the mechanical rigidity of the resultant gel by a factor of 90 in some cases, while retaining the gel’s shear thin-recovery behavior. We further investigate how factors such as polymerization time, dopamine concentration and peptide concentration alter the mechanical properties of the resultant gel. The hybrid peptide–dopamine gel systems were characterized using rheological measurements, circular dichroism spectroscopy and transmission electron microscopy. Overall, triggering peptide gelation in the presence of dopamine represents a simple yet powerful approach to modulate the viscoelastic mechanical properties of peptide-based gels. Full article
(This article belongs to the Special Issue Bioinspired Peptide/Protein Nanomaterials: Form-Structure-Function)
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11 pages, 3872 KiB  
Article
Heterotypic Supramolecular Hydrogels Formed by Noncovalent Interactions in Inflammasomes
by Adrianna N. Shy, Huaimin Wang, Zhaoqianqi Feng and Bing Xu
Molecules 2021, 26(1), 77; https://doi.org/10.3390/molecules26010077 - 26 Dec 2020
Cited by 4 | Viewed by 2567
Abstract
The advance of structural biology has revealed numerous noncovalent interactions between peptide sequences in protein structures, but such information is less explored for developing peptide materials. Here we report the formation of heterotypic peptide hydrogels by the two binding motifs revealed by the [...] Read more.
The advance of structural biology has revealed numerous noncovalent interactions between peptide sequences in protein structures, but such information is less explored for developing peptide materials. Here we report the formation of heterotypic peptide hydrogels by the two binding motifs revealed by the structures of an inflammasome. Specifically, conjugating a self-assembling motif to the positively or negatively charged peptide sequence from the ASCPYD filaments of inflammasome produces the solutions of the peptides. The addition of the peptides of the oppositely charged and complementary peptides to the corresponding peptide solution produces the heterotypic hydrogels. Rheology measurement shows that ratios of the complementary peptides affect the viscoelasticity of the resulted hydrogel. Circular dichroism indicates that the addition of the complementary peptides results in electrostatic interactions that modulate self-assembly. Transmission electron microscopy reveals that the ratio of the complementary peptides controls the morphology of the heterotypic peptide assemblies. This work illustrates a rational, biomimetic approach that uses the structural information from the protein data base (PDB) for developing heterotypic peptide materials via self-assembly. Full article
(This article belongs to the Special Issue Bioinspired Peptide/Protein Nanomaterials: Form-Structure-Function)
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