Biomimetic Approaches in Healthcare—Innovations Inspired by Nature: 2nd Edition

A special issue of Biomimetics (ISSN 2313-7673). This special issue belongs to the section "Development of Biomimetic Methodology".

Deadline for manuscript submissions: 30 May 2025 | Viewed by 740

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Special Issue Information

Dear Colleagues,

This Special Issue, entitled "Biomimetic Approaches in Healthcare—Innovations Inspired by Nature", explores the innovative intersection of healthcare and nature-inspired solutions. This collection of research articles delves into the emerging field of biomimetics, where scientists and healthcare professionals draw inspiration from the natural world to develop groundbreaking healthcare technologies and strategies. By mimicking biological processes, structures, and systems found in the environment, researchers aim to create more effective and sustainable solutions for healthcare challenges. This Special Issue features contributions that showcase how biomimetic approaches are revolutionizing medical diagnostics, treatment modalities, and healthcare practices. From bio-inspired materials for regenerative medicine to nature-inspired algorithms for healthcare data analysis, this Special Issue highlights the diverse applications of biomimetics in improving healthcare outcomes.

Prof. Dr. Vicente Javier Clemente-Suárez
Prof. Dr. Ana Isabel Beltrán-Velasco
Guest Editors

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Keywords

  • biomimetics
  • healthcare innovations
  • nature-inspired solutions
  • medical diagnostics
  • regenerative medicine
  • bio-inspired materials
  • healthcare data analysis
  • natural algorithms
  • biologically inspired technology
  • sustainable healthcare

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Research

28 pages, 7444 KiB  
Article
Exploring the Potential of Biomimetic Peptides in Targeting Fibrillar and Filamentous Alpha-Synuclein—An In Silico and Experimental Approach to Parkinson’s Disease
by Sophia A. Frantzeskos, Mary A. Biggs and Ipsita A. Banerjee
Biomimetics 2024, 9(11), 705; https://doi.org/10.3390/biomimetics9110705 - 18 Nov 2024
Viewed by 619
Abstract
Alpha-synuclein (ASyn) is a protein that is known to play a critical role in Parkinson’s disease (PD) due to its propensity for misfolding and aggregation. Furthermore, this process leads to oxidative stress and the formation of free radicals that cause neuronal damage. In [...] Read more.
Alpha-synuclein (ASyn) is a protein that is known to play a critical role in Parkinson’s disease (PD) due to its propensity for misfolding and aggregation. Furthermore, this process leads to oxidative stress and the formation of free radicals that cause neuronal damage. In this study, we have utilized a biomimetic approach to design new peptides derived from marine natural resources. The peptides were designed using a peptide scrambling approach where antioxidant moieties were combined with fibrillary inhibition motifs in order to design peptides that would have a dual targeting effect on ASyn misfolding. Of the 20 designed peptides, 12 were selected for examining binding interactions through molecular docking and molecular dynamics approaches, which revealed that the peptides were binding to the pre-NAC and NAC (non-amyloid component) domain residues such as Tyr39, Asn65, Gly86, and Ala85, among others. Because ASyn filaments derived from Lewy body dementia (LBD) have a different secondary structure compared to pathogenic ASyn fibrils, both forms were tested computationally. Five of those peptides were utilized for laboratory validation based on those results. The binding interactions with fibrils were confirmed using surface plasmon resonance studies, where EQALMPWIWYWKDPNGS, PYYYWKDPNGS, and PYYYWKELAQM showed higher binding. Secondary structural analyses revealed their ability to induce conformational changes in ASyn fibrils. Additionally, PYYYWKDPNGS and PYYYWKELAQM also demonstrated antioxidant properties. This study provides insight into the binding interactions of varying forms of ASyn implicated in PD. The peptides may be further investigated for mitigating fibrillation at the cellular level and may have the potential to target ASyn. Full article
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