Supramolecular peptide hydrogels (SPHs) consist of peptides containing hydrogelators and functional epitopes, which can first self-assemble into nanofibers and then physically entangle together to form dynamic three-dimensional networks. Their porous structures, excellent bioactivity, and high dynamicity, similar to an extracellular matrix (ECM), have great potential in artificial ECM. The properties of the hydrogel are largely dependent on peptides. The noncovalent interactions among hydrogelators drive the formation of assemblies and further transition into hydrogels, while bioactive epitopes modulate cell-cell and cell-ECM interactions. Therefore, SPHs can support cell growth, making them ideal biomaterials for ECM mimics. This Review outlines the classical molecular design of SPHs from hydrogelators to functional epitopes and summarizes the recent advancements of SPHs as artificial ECMs in nervous system repair, wound healing, bone and cartilage regeneration, and organoid culture. This emerging SPH platform could provide an alternative strategy for developing more effective biomaterials for tissue engineering.
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http://dx.doi.org/10.1021/acs.biomac.4c00971 | DOI Listing |
J Mater Chem B
January 2025
School of Materials Science and Engineering, University of New South Wales (UNSW Sydney), Sydney, NSW 2052, Australia.
Most synthetic hydrogels are formed through radical polymerization to yield a homogenous covalent meshwork. In contrast, natural hydrogels form through mechanisms involving both covalent assembly and supramolecular interactions. In this communication, we expand the capabilities of covalent poly(ethylene glycol) (PEG) networks through co-assembly of supramolecular peptide nanofibers.
View Article and Find Full Text PDFJ Am Chem Soc
January 2025
Engineering Research Center of Advanced Rare Earth Materials (Ministry of Education), Department of Chemistry, Tsinghua University, Beijing 100084, China.
Hierarchical structures are essential in natural adhesion systems. Replicating these in synthetic adhesives is challenging due to intricate molecular mechanisms and multiscale processes. Here, we report three phosphorylated peptides featuring a hydrophobic self-assembly motif linked to a hydrophilic phosphorylated sequence (pSGSS), forming peptide fibril nanoframeworks.
View Article and Find Full Text PDFACS Nano
January 2025
State Key Laboratory of Physical Chemistry of Solid Surface, Key Laboratory of Chemical Biology of Fujian Province, Collaborative Innovation Center of Chemistry for Energy Materials (iChEM), Innovation Laboratory for Sciences and Technologies of Energy Materials of Fujian Province (IKKEM), College of Chemistry and Chemical Engineering, Xiamen University, Xiamen 361005, P. R. China.
The assembly of peptides is generally mediated by liquid-liquid phase separation, which enables control over assembly kinetics, final structure, and functions of peptide-based supramolecular materials. Modulating phase separation can alter the assembly kinetics of peptides by changing solvents or introducing external fields. Herein, we demonstrate that the assembly of peptides can be effectively catalyzed by complex coacervates.
View Article and Find Full Text PDFFood Res Int
January 2025
Institut Numecan, INSERM, INRAE, Univ Rennes, Rennes, France. Electronic address:
Dietary protein reduces energy intake in following meals by signaling directly or indirectly to the brain. We recently observed differences in plasma amino acid kinetics and intra-gastric behavior between micellar casein (MC) and sodium caseinate (SC) in pigs, two factors that impact food intake. Our objective was to clarify whether the supramolecular structure of casein, given as a preload to pigs, impacts on subsequent food intake.
View Article and Find Full Text PDFCurr Opin Chem Biol
January 2025
Centro Singular de Investigación en Química Biolóxica e Materiais Moleculares (CiQUS), Departamento de Química Orgánica, Universidade de Santiago de Compostela, 15705, Santiago de Compostela, Spain. Electronic address:
Transmembrane ion exchange controls biological functions and is essential for life. Over the years, a great variety of nature-inspired artificial ion channels and carriers have been synthesized to control and promote ion exchange across biological membranes. In this context, peptides emerged as ideal scaffolds for synthetic ion channels due to their biocompatibility, accessibility and chemical versatility.
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