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Editorial Board Members’ Collection Series: Biomimetics of Materials, Functions, Structures...
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Editorial Board Members’ Collection Series: Biomimetics of Materials, Functions, Structures and Processes 2024

A special issue of Biomimetics (ISSN 2313-7673). This special issue belongs to the section "Biomimetics of Materials and Structures".

Deadline for manuscript submissions: 1 April 2025 | Viewed by 2970

Special Issue Editors

Prof. Dr. Thomas Speck

E-Mail Website
Guest Editor
Plant Biomechanics Group, Botanic Garden, Faculty of Biology, University of Freiburg, Schänzlestraße 1, D 79104 Freiburg, Germany
Interests: functional morphology and biomechanics of plants; plant–animal interactions; bioinspired materials systems, structures, and surfaces; phylogeny of plants and functional structures; paleobotany; scientific education and training in Botanic Gardens
Special Issues, Collections and Topics in MDPI journals
Prof. Dr. Candan Tamerler

E-Mail Website
Guest Editor
Department of Mechanical Engineering, Institute for Bioengineering Research, University of Kansas, 1530 W 15th St Learned Hall Lawrence, Lawrence, KS 66045, USA
Interests: bio-nano interfaces; bio-nanotechnology; surfaces; biomaterials; tissue engineering; nano-biosensors; biocatalysis molecular biomimetics; bioengineering
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

We are pleased to announce a new Special Issue, titled “Editorial Board Members’ Collection Series: Biomimetics of Materials, Functions, Structures and Processes 2024”, which will collect papers invited by our Editorial Board Members.

The aim of this Special Issue is to provide a venue for networking and communication between Biomimetics and scholars in the fields of biomimetic materials addressing function, structures and processes. This Special Issue will include papers offering a fundamental understanding of biological materials, translating nature’s design principles in solving engineering challenges through innovative materials with fascinating structures, properties and functions that combine bio-based, bio-hybrid and synthetic approaches and processes enabling us to mimic biological structures and introduce biological functions. All papers will be published open access following peer review.

Prof. Dr. Thomas Speck
Prof. Dr. Candan Tamerler
Guest Editors

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. Biomimetics is an international peer-reviewed open access monthly 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 2200 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.

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  • e-Book format: Special Issues with more than 10 articles can be published as dedicated e-books, ensuring wide and rapid dissemination.

Further information on MDPI's Special Issue policies can be found here.

Published Papers (4 papers)

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13 pages, 2216 KiB  
Article
Characterization of Gramicidin A in Triblock and Diblock Polymersomes and Hybrid Vesicles via Continuous Wave Electron Paramagnetic Resonance Spectroscopy
by Emma A. Gordon, Indra D. Sahu, Joel R. Fried and Gary A. Lorigan
Biomimetics 2025, 10(3), 154; https://doi.org/10.3390/biomimetics10030154 - 2 Mar 2025
Viewed by 398
Abstract
Studying membrane proteins in a native environment is crucial to understanding their structural and/or functional studies. Often, widely accepted mimetic systems have limitations that prevent the study of some membrane proteins. Micelles, bicelles, and liposomes are common biomimetic systems but have problems with [...] Read more.
Studying membrane proteins in a native environment is crucial to understanding their structural and/or functional studies. Often, widely accepted mimetic systems have limitations that prevent the study of some membrane proteins. Micelles, bicelles, and liposomes are common biomimetic systems but have problems with membrane compatibility, limited lipid composition, and heterogeneity. To overcome these limitations, polymersomes and hybrid vesicles have become popular alternatives. Polymersomes form from amphiphilic triblock or diblock copolymers and are considered more robust than liposomes. Hybrid vesicles are a combination of lipids and block copolymers that form vesicles composed of a mixture of the two. These hybrid vesicles are appealing because they have the native lipid environment of bilayers but also the stability and customizability of polymersomes. Gramicidin A was incorporated into these polymersomes and characterized using continuous wave electron paramagnetic resonance (CW-EPR) and transmission electron microscopy (TEM). EPR spectroscopy is a powerful biophysical technique used to study the structure and dynamic properties of membrane proteins in their native environment. Spectroscopic studies of gramicidin A have been limited to liposomes; in this study, the membrane peptide is studied in both polymersomes and hybrid vesicles using CW-EPR spectroscopy. Lineshape analysis of spin-labeled gramicidin A revealed linewidth broadening, suggesting that the thicker polymersome membranes restrict the motion of the spin label more when compared to liposome membranes. Statement of Significance: Understanding membrane proteins’ structures and functions is critical in the study of many diseases. In order to study them in a native environment, membrane mimetics must be developed that can be suitable for obtaining superior biophysical data quality to characterize structural dynamics while maintaining their native functions and structures. Many currently widely accepted methods have limitations, such as a loss of native structure and function, heterogeneous vesicle formation, restricted lipid types for the vesicle formation for many proteins, and experimental artifacts, which leaves rooms for the development of new biomembrane mimetics. The triblock and diblock polymersomes and hybrid versicles utilized in this study may overcome these limitations and provide the stability and customizability of polymersomes, keeping the biocompatibility and functionality of liposomes for EPR studies of membrane proteins. Full article
(This article belongs to the Special Issue Editorial Board Members’ Collection Series: Biomimetics of Materials, Functions, Structures and Processes 2024)
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17 pages, 2773 KiB  
Article
Probing Solid-Binding Peptide Self-Assembly Kinetics Using a Frequency Response Cooperativity Model
by Taylor Bader, Kyle Boone, Chris Johnson, Cindy L. Berrie and Candan Tamerler
Biomimetics 2025, 10(2), 107; https://doi.org/10.3390/biomimetics10020107 - 12 Feb 2025
Viewed by 640
Abstract
Biomolecular adsorption has great significance in medical, environmental, and technological processes. Understanding adsorption equilibrium and binding kinetics is essential for advanced process implementation. This requires identifying intrinsic determinants that predict optimal adsorption properties at bio–hybrid interfaces. Solid-binding peptides (SBPs) have targetable intrinsic properties [...] Read more.
Biomolecular adsorption has great significance in medical, environmental, and technological processes. Understanding adsorption equilibrium and binding kinetics is essential for advanced process implementation. This requires identifying intrinsic determinants that predict optimal adsorption properties at bio–hybrid interfaces. Solid-binding peptides (SBPs) have targetable intrinsic properties involving peptide–peptide and peptide–solid interactions, which result in high-affinity material-selective binding. Atomic force microscopy investigations confirmed this complex interplay of multi-step peptide assemblies in a cooperative modus. Yet, most studies report adsorption properties of SBPs using non-cooperative or single-step adsorption models. Using non-cooperative kinetic models for predicting cooperative self-assembly behavior creates an oversimplified view of peptide adsorption, restricting implementing SBPs beyond their current use. To address these limitations and provide insight into surface-level events during self-assembly, a novel method, the Frequency Response Cooperativity model, was developed. This model iteratively fits adsorption data through spectral analysis of several time-dependent kinetic parameters. The model, applied to a widely used gold-binding peptide data obtained using a quartz crystal microbalance with dissipation, verified multi-step assembly. Peak deconvolution of spectral plots revealed distinct differences in the size and distribution of the kinetic rates present during adsorption across the concentrations. This approach provides new fundamental insights into the intricate dynamics of self-assembly of biomolecules on surfaces. Full article
(This article belongs to the Special Issue Editorial Board Members’ Collection Series: Biomimetics of Materials, Functions, Structures and Processes 2024)
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15 pages, 3355 KiB  
Article
Bio-Inspired Sutures: Localizing Damage by Isolating Strain Energy
by Diana A. Chen and Melissa M. Gibbons
Biomimetics 2025, 10(2), 102; https://doi.org/10.3390/biomimetics10020102 - 11 Feb 2025
Viewed by 486
Abstract
This study draws upon bio-inspiration from anatomical sutures found in hard structures, such as turtle shells, to explore if impact energy can be dissipated through geometric parameterization rather than relying on energy-absorbing materials. While previous finite element analysis studies identified optimal dovetail suture [...] Read more.
This study draws upon bio-inspiration from anatomical sutures found in hard structures, such as turtle shells, to explore if impact energy can be dissipated through geometric parameterization rather than relying on energy-absorbing materials. While previous finite element analysis studies identified optimal dovetail suture geometries for maximizing the global stiffness and toughness of archway structures, this paper explores how different suture geometries might optimize localization effects through segmentation to isolate damage caused by the propagation of strain energy. We compare the global toughness of each suture geometry to its scaling factor, defined as the ratio of strain energy in the center segment(s) of the archway over the total strain energy absorbed during deformation, normalized by the expected strain energy consistent with uniform volumetric distribution. Our findings indicate that the scaling factor tended to correlate positively with global toughness, suggesting that suture geometries that performed well globally would also exhibit the localization effect. However, there is some nuance in selecting suture geometries that perform well for both metrics, as well as ensuring that geometries that perform well for one type of segmentation are still structurally sound in others, due to little control over where impact may occur, relative to the location of a suture, in real scenarios. Full article
(This article belongs to the Special Issue Editorial Board Members’ Collection Series: Biomimetics of Materials, Functions, Structures and Processes 2024)
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15 pages, 24047 KiB  
Article
Enhancing CO2 Adsorption on MgO: Insights into Dopant Selection and Mechanistic Pathways
by Shunnian Wu, W. P. Cathie Lee, Hashan N. Thenuwara, Xu Li and Ping Wu
Biomimetics 2025, 10(1), 9; https://doi.org/10.3390/biomimetics10010009 - 27 Dec 2024
Viewed by 867
Abstract
Inspired by our recent success in designing CO2-phobic and CO2-philic domains on nano-MgO for effective CO2 adsorption, our ongoing efforts focus on incorporating dopants into pristine MgO to further enhance its CO2 adsorption capabilities. However, a clear [...] Read more.
Inspired by our recent success in designing CO2-phobic and CO2-philic domains on nano-MgO for effective CO2 adsorption, our ongoing efforts focus on incorporating dopants into pristine MgO to further enhance its CO2 adsorption capabilities. However, a clear set of guidelines for dopant selection and a holistic understanding of the underlying mechanisms is still lacking. In our investigation, we combined first-principles calculations with experimental approaches to explore the crystal and electronic structural changes in MgO doped with high-valence elements (Al, C, Si, and Ti) and their interactions with CO2. Our findings unveiled two distinct mechanisms for CO2 capture: Ti-driven catalytic CO2 decomposition and CO2 polarization induced by Al, C, and Si. Ti doping induced outward Ti atom displacement and structural distortion, facilitating CO2 dissociation, whereas C doping substantially bolstered the electron donation capacity and CO2 adsorption energy. Pristine and C-doped MgO engaged CO2 through surface O atoms, while Al-, Si-, and Ti-doped MgO predominantly relied on dopant–O atom interactions. Our comprehensive research, integrating computational modeling and experimental work supported by scanning electron microscopy and thermal gravimetric analysis, confirmed the superior CO2 adsorption capabilities of C-doped MgO. This yielded profound insights into the mechanisms and principles that govern dopant selection and design. Full article
(This article belongs to the Special Issue Editorial Board Members’ Collection Series: Biomimetics of Materials, Functions, Structures and Processes 2024)
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