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Functionalised Self Assembling Peptides in Multi-Component Systems, Biomedical Materials with Added Complexity

A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Materials Science".

Deadline for manuscript submissions: closed (31 December 2019) | Viewed by 4568

Special Issue Editor

Department of Oral Biology, University of Leeds, Leeds LS9 7TF, UK
Interests: soft matter; peptide self-assembly; functional biomimetic scaffolds and regenerative dentistry

Special Issue Information

Dear Colleagues,

The formation of well-organised assemblies through revisable non-covalent interactions defines the phenomena of self-assembly. The range of structures formed through this process often transcends typical-length scales; basic molecular building blocks can be triggered to form kinetically or thermodynamically stable hierarchical assemblies at the nanoscale, mesoscale, and macroscale, giving rise to novel materials. Indeed, the rational design of peptidic biomolecules that manipulate non-covalent interactions to form these supramolecular structures has given rise to a class of materials for use in regenerative medicine.

Peptide based self-assemblies, inspired by amino acid sequences found in nature, are able to from three dimensional matrices. In an unadulterated form, these matrices have a range of applications within the fields of tissue engineering and regenerative medicine. The ability to control the surface chemistry and the overall nature of the scaffold has yielded well-documented success in these areas. However, combining self-assembling peptides (SAPs) with other moieties or functionalising the SAPs themselves can modify their chemistries and bioactivities, allowing for the development of multi-component systems exhibiting enhanced physical and biological properties that can be utilised for patient benefit.

This Special Issue aims to explore peptide based multi-component systems for use in tissue engineering and regenerative medicine. Papers related to the study and/or applications of self-assembled peptides functionalised with other moieties and their potential biomedical applications are welcomed.

Dr. Robert Philip Wynn Davies
Guest Editor

Manuscript Submission Information

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Keywords

  • Supramolecular assemblies
  • Self-assembling peptides
  • Multi component systems
  • Functionalized peptides
  • Scaffolds
  • Hydrogels
  • Biomimetic
  • Biomedical applications
  • Hard and soft tissue engineering

Published Papers (1 paper)

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Review

23 pages, 6350 KiB  
Review
Peptidic Antifreeze Materials: Prospects and Challenges
by Romà Surís-Valls and Ilja K. Voets
Int. J. Mol. Sci. 2019, 20(20), 5149; https://0-doi-org.brum.beds.ac.uk/10.3390/ijms20205149 - 17 Oct 2019
Cited by 21 | Viewed by 4225
Abstract
Necessitated by the subzero temperatures and seasonal exposure to ice, various organisms have developed a remarkably effective means to survive the harsh climate of their natural habitats. Their ice-binding (glyco)proteins keep the nucleation and growth of ice crystals in check by recognizing and [...] Read more.
Necessitated by the subzero temperatures and seasonal exposure to ice, various organisms have developed a remarkably effective means to survive the harsh climate of their natural habitats. Their ice-binding (glyco)proteins keep the nucleation and growth of ice crystals in check by recognizing and binding to specific ice crystal faces, which arrests further ice growth and inhibits ice recrystallization (IRI). Inspired by the success of this adaptive strategy, various approaches have been proposed over the past decades to engineer materials that harness these cryoprotective features. In this review we discuss the prospects and challenges associated with these advances focusing in particular on peptidic antifreeze materials both identical and akin to natural ice-binding proteins (IBPs). We address the latest advances in their design, synthesis, characterization and application in preservation of biologics and foods. Particular attention is devoted to insights in structure-activity relations culminating in the synthesis of de novo peptide analogues. These are sequences that resemble but are not identical to naturally occurring IBPs. We also draw attention to impactful developments in solid-phase peptide synthesis and ‘greener’ synthesis routes, which may aid to overcome one of the major bottlenecks in the translation of this technology: unavailability of large quantities of low-cost antifreeze materials with excellent IRI activity at (sub)micromolar concentrations. Full article
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