Molecular self-assembly has paved the way to create novel, supramolecular, functional biomaterials. Peptide-based biomaterials are gaining interest as a result of their programmability, biodegradability, and bioresorbability. Further, unlike polymeric materials, peptides can be made monodisperse with precise control over sequence, chain length, and stereochemistry. Peptide-based viscoelastic matrices have been designed and characterized for various biomedical applications, such as tissue engineering scaffolds or drug delivery vehicles. The 'holy grail' in designing an ideal tissue engineering scaffold lies in mimicking the cues of the tissue's natural extracellular matrix (ECM). Some of the key elements of ECM that are incorporated into these peptide scaffolds include cell-adhesive and protease-sensitive sequences for enhanced cell-cell and cell-biomaterial interactions. Peptide-based viscoelastic matrices can also be engineered with drug carrying protease-sensitive sequences for controlled and site-specific drug delivery. Molecular-level engineering of simple oligopeptide modules can be used to control the position and density of the bio-mimetic functionalities in the supramolecular structures, which demonstrates the power of the 'bottom-up' approach in self-assembly.
Download full-text PDF |
Source |
---|---|
http://dx.doi.org/10.2165/00063030-200620050-00001 | DOI Listing |
Small
January 2025
Leicester Institute for Pharmaceutical Innovation, Leicester School of Pharmacy, De Montfort University, The Gateway, Leicester, LE1 9BH, UK.
Guiding molecular assembly of peptides into rationally engineered nanostructures remains a major hurdle against the development of functional peptide-based nanomaterials. Various non-covalent interactions come into play to drive the formation and stabilization of these assemblies, of which electrostatic interactions are key. Here, the atomistic mechanisms by which electrostatic interactions contribute toward controlling self-assembly and lateral association of ultrashort β-sheet forming peptides are deciphered.
View Article and Find Full Text PDFACS Appl Energy Mater
December 2024
Department of Chemical and Environmental Process Engineering, Faculty of Chemical Technology and Biotechnology, Budapest University of Technology and Economics, Műegyetem rkp. 3, Budapest H-1111, Hungary.
Amphiphilic copolymers of comb-like poly(poly(ethylene glycol) methacrylate) (PPEGMA) with methyl methacrylate (MMA) synthesized by one-pot atom transfer radical polymerization were mixed with lithium bis (trifluoromethanesulfonyl) imide salt to formulate dry solid polymer electrolytes (DSPE) for semisolid-state Li-ion battery applications. The PEO-type side chain length (EO monomer's number) in the PEGMA macromonomer units was varied, and its influence on the mechanical and electrochemical characteristics was investigated. It was found that the copolymers, due to the presence of PMMA segments, possess viscoelastic behavior and less change in mechanical properties than a PEO homopolymer with 100 kDa molecular weight in the investigated temperature range.
View Article and Find Full Text PDFJ Control Release
December 2024
Hunan Provincial Key Laboratory of Animal Models and Molecular Medicine, State Key Laboratory of Chemo/Bio-Sensing and Chemometrics, School of Biomedical Sciences, Hunan University, Changsha 410082, Hunan, PR China; Greater Bay Area Institute for Innovation, Hunan University, Guangzhou 511300, Guangdong, PR China. Electronic address:
Vitreoretinal diseases pose significant threats to vision, often requiring vitrectomy and substitution of vitreous humor to restore ocular structure and visual function. However, existing substitutes have limitations that compromise patient outcomes. Supramolecular hydrogels, particularly peptide-based formulations, have emerged as promising alternatives due to their superior optical clarity, biocompatibility, and viscoelasticity.
View Article and Find Full Text PDFBiomacromolecules
June 2024
Department of Medicinal Chemistry, National Institute of Pharmaceutical Education and Research (NIPER) Mohali, S.A.S. Nagar (Mohali) 160062, India.
A majority of short peptide (≤7 amino acids) hydrogels are primarily assembled via cross β-structure formation. In contrast to the natural trend, herein, we report the formation of supramolecular hydrogel from the ultrashort hybrid folded peptide composed of canonical α-amino acid and noncanonical γ-amino acid, Fmoc-γPhe-Phe-OH. The designed hybrid peptide hydrogel is composed of entangled fibers, has viscoelastic properties, exhibits proteolytic stability, and exhibits cytocompatibility with L929 fibroblast cells.
View Article and Find Full Text PDFSoft Matter
March 2024
Department of Chemistry, University of Toronto, 80 St. George Street, M5S 3H6, Toronto, Canada.
Peptide self-assembly has been highly studied to understand the pathways in forming higher order structures along with the development and application of resulting hydrogel materials. Driven by noncovalent interactions, peptide hydrogels are stimuli-responsive to any addition to its gelling conditions. Here, a Phe-His based peptide, C-FH(Trt)-OH, was synthesized and characterized with H NMR, FT-IR, MS, UV-vis spectroscopies and elemental analysis.
View Article and Find Full Text PDFEnter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!