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Biopolymer Networks
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Biopolymer Networks

A special issue of Polymers (ISSN 2073-4360). This special issue belongs to the section "Biobased and Biodegradable Polymers".

Deadline for manuscript submissions: closed (15 June 2024) | Viewed by 3686

Special Issue Editor

Prof. Dr. Rae Robertson-Anderson

E-Mail Website
Guest Editor
Physics and Biophysics Department, University of San Diego, San Diego, CA, USA
Interests: soft matter; active matter; biopolymers; microrheology; optical tweezers; DNA; cytoskeleton

Special Issue Information

Dear Colleagues,

Biopolymer networks are the topic of fervent interdisciplinary research in physics, biology, chemistry, engineering, and materials science. This Special Issue will have a broad and interdisciplinary scope, with a forward-looking perspective on research on biopolymer networks. Why are researchers interested in biopolymer networks? Polymer Physics: Because biopolymers naturally exist in a range of stiffnesses, sizes, and topologies, and they serve as model systems for investigating perplexing problems in polymer physics, such as shortcomings of the reptation model for entangled polymer networks. Materials Science: Researchers are capitalizing on billions of years of biological evolution to  design networks of biopolymers that exhibit emergent non-equilibrium material properties not possible with synthetic analogs. Soft and Active Matter: Biopolymer networks exhibit rich and tunable viscoelastic properties that can be precisely tuned by the properties, concentrations, and interactions of the comprising polymers. Moreover, molecular motors and enzymes can drive biopolymer networks to restructure, flow, and coarsen. As such, biopolymer networks continue to be the paradigmatic testbed for the design and understanding of soft and active matter. Cellular Biology: The physical properties and interactions between proteins, DNA, RNA, lipids, and polysaccharides, all biopolymers that crowd biological cells, drive most processes in living organisms. This collection will feature research encompassing these diverse perspectives.

Prof. Dr. Rae Robertson-Anderson
Guest Editor

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

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. Polymers 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

  • biopolymers
  • entangled polymers
  • cytoskeleton
  • DNA
  • semiflexible polymers
  • microrheology
  • crowding
  • viscoelasticity
  • active matter
  • soft matter

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Published Papers (2 papers)

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Research

11 pages, 2279 KiB  
Article
Reversibility in the Physical Properties of Agarose Gels following an Exchange in Solvent and Non-Solvent
by Denis C. D. Roux, François Caton, Isabelle Jeacomine, Guillaume Maîtrejean and Marguerite Rinaudo
Polymers 2024, 16(6), 811; https://doi.org/10.3390/polym16060811 - 14 Mar 2024
Cited by 2 | Viewed by 1526
Abstract
Agarose forms a homogeneous thermoreversible gel in an aqueous solvent above a critical polymer concentration. Contrary to the prevailing consensus, recent confirmations indicate that agarose gels are also stable in non-solvents like acetone and ethanol. A previous study compared gel characterisations and behaviours [...] Read more.
Agarose forms a homogeneous thermoreversible gel in an aqueous solvent above a critical polymer concentration. Contrary to the prevailing consensus, recent confirmations indicate that agarose gels are also stable in non-solvents like acetone and ethanol. A previous study compared gel characterisations and behaviours in water and ethanol, discussing the gelation mechanism. In the current work, the ethanol gel is exchanged with water to explore the potential reversibility of the displacement of water in agarose. Initially, the structure is characterised using 1H NMR in DMSO-d6 and D2O solvents. Subsequently, a very low yield (0.04) of methyl substitution per agarobiose unit is determined. The different gels after stabilisation are characterised using rheology, and their physical properties are compared based on the solvent used. The bound water molecules, acting as plasticizers in aqueous medium, are likely removed during the exchange process with ethanol, resulting in a stronger and more fragile gel. Next, the gel obtained after the second exchange from ethanol back to water is compared with the initial gel prepared in water. This is the first time where such gel has been characterised without undergoing a phase transition when switching from a good solvent to a non-solvent, and vice versa, thereby testing the reversibility of the solvent exchange. Reversibility of this behaviour is demonstrated through swelling and rheology experiments. This study extends the application of agarose in chromatography and electrophoresis. Full article
(This article belongs to the Special Issue Biopolymer Networks)
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16 pages, 2103 KiB  
Article
Nonlinear Microscale Mechanics of Actin Networks Governed by Coupling of Filament Crosslinking and Stabilization
by Mike E. Dwyer, Rae M. Robertson-Anderson and Bekele J. Gurmessa
Polymers 2022, 14(22), 4980; https://doi.org/10.3390/polym14224980 - 17 Nov 2022
Cited by 2 | Viewed by 1653
Abstract
Actin plays a vital role in maintaining the stability and rigidity of biological cells while allowing for cell motility and shape change. The semiflexible nature of actin filaments—along with the myriad actin-binding proteins (ABPs) that serve to crosslink, bundle, and stabilize filaments—are central [...] Read more.
Actin plays a vital role in maintaining the stability and rigidity of biological cells while allowing for cell motility and shape change. The semiflexible nature of actin filaments—along with the myriad actin-binding proteins (ABPs) that serve to crosslink, bundle, and stabilize filaments—are central to this multifunctionality. The effect of ABPs on the structural and mechanical properties of actin networks has been the topic of fervent investigation over the past few decades. Yet, the combined impact of filament stabilization, stiffening and crosslinking via ABPs on the mechanical response of actin networks has yet to be explored. Here, we perform optical tweezers microrheology measurements to characterize the nonlinear force response and relaxation dynamics of actin networks in the presence of varying concentrations of α-actinin, which transiently crosslinks actin filaments, and phalloidin, which stabilizes filamentous actin and increases its persistence length. We show that crosslinking and stabilization can act both synergistically and antagonistically to tune the network resistance to nonlinear straining. For example, phalloidin stabilization leads to enhanced elastic response and reduced dissipation at large strains and timescales, while the initial microscale force response is reduced compared to networks without phalloidin. Moreover, we find that stabilization switches this initial response from that of stress stiffening to softening despite the increased filament stiffness that phalloidin confers. Finally, we show that both crosslinking and stabilization are necessary to elicit these emergent features, while the effect of stabilization on networks without crosslinkers is much more subdued. We suggest that these intriguing mechanical properties arise from the competition and cooperation between filament connectivity, bundling, and rigidification, shedding light on how ABPs with distinct roles can act in concert to mediate diverse mechanical properties of the cytoskeleton and bio-inspired polymeric materials. Full article
(This article belongs to the Special Issue Biopolymer Networks)
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