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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 |
Nat Nanotechnol
September 2025
Department of Bioengineering, Rice University, Houston, TX, USA.
Maintaining safe and potent drug levels in vivo is challenging. Multidomain peptides assemble into supramolecular hydrogels with a well-defined, highly porous nanostructure that makes them attractive for drug delivery. However, their ability to extend release is typically limited by rapid drug diffusion.
View Article and Find Full Text PDFACS Appl Mater Interfaces
September 2025
Department of Materials Science and Engineering, Gwangju Institute of Science and Technology (GIST), Gwangju 61005, Republic of Korea.
Cyclic peptides (CPs) are versatile building blocks whose conformational constraints foster ordered supramolecular architectures with potential in biomedicine, nanoelectronics, and catalysis. Herein, we report the development of biomimetic antifreeze materials by conjugating CPs bearing ice-binding residues to 4-arm polyethylene glycol (PEG) via click chemistry. The concentration-dependent self-assembly of these CP-PEG conjugates induces programmable morphological transitions, forming nanotube networks above the critical aggregation concentration (CAC) and two-dimensional nanosheet networks near the CAC.
View Article and Find Full Text PDFAtherosclerosis
September 2025
Division of Biotherapeutics, Leiden Academic Centre for Drug Research, Leiden University, Leiden, the Netherlands. Electronic address:
Background And Aim: Atherosclerosis has an auto-immune component driven by self-reactive T and B cells. Identifying their antigenic drivers may lead to new diagnosis and treatment approaches. Here, we aim to identify immunogenic T cell epitopes derived from atherosclerosis-relevant proteins such as ApoB100 by studying the repertoire of peptides presented by HLA in human plaques.
View Article and Find Full Text PDFAdv Healthc Mater
September 2025
Institute for Complex Molecular Systems, Eindhoven University of Technology, Eindhoven, 5600 MB, the Netherlands.
Intestinal organoids are three-dimensional cellular structures that are cultured in laminin-rich Matrigel, yielding organoids with correct, basal-out polarity. Removal of Matrigel results in organoids with reversed, apical-out polarity, demonstrating its vital role. However, Matrigel's composition is ill-defined, and its pathogenic origin poses challenges in reproducibility.
View Article and Find Full Text PDFJ Colloid Interface Sci
August 2025
Wenzhou Institute, University of Chinese Academy of Sciences, Wenzhou 325001, China; Terahertz Technology Innovation Research Institute, Terahertz Spectrum and Imaging Technology Cooperative Innovation Center, Shanghai Key Lab of Modern Optical System, School of Optical-Electrical and Computer Engin
Precise engineering of hydrophobic microenvironments in synthetic peptide-catecholamine co-assemblies remains challenging for tunable fluorescence. Hierarchical nanostructures were constructed through sequence-specific peptide encoding (GYK tripeptide and Ac-IIIGYK-NH₂ hexapeptide) and co-assembly with catecholamines of graded hydrophobicity. Structural dynamics were analyzed via molecular simulations, HPLC, AFM, and spectroscopy.
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