Artificial composites designed to mimic the structure and properties of native extracellular matrix may lead to acellular materials for soft tissue repair and replacement, which display mechanical strength, stiffness, and resilience resembling native tissue. We describe the fabrication of thin lamellae consisting of continuous collagen microfiber embedded at controlled orientations and densities in a recombinant elastin-like protein polymer matrix. Multilamellar stacking affords flexible, protein-based composite sheets whose properties are dependent upon both the elastomeric matrix and collagen content and organization. Sheets are produced with properties that range over 13-fold in elongation to break (23-314%), six-fold in Young's modulus (5.3-33.1 MPa), and more than two-fold in tensile strength (1.85-4.08 MPa), exceeding that of a number of native human tissues, including urinary bladder, pulmonary artery, and aorta. A sheet approximating the mechanical response of human abdominal wall fascia is investigated as a fascial substitute for ventral hernia repair. Protein-based composite patches prevent hernia recurrence in Wistar rats over an 8-week period with new tissue formation and sustained structural integrity.
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http://dx.doi.org/10.1016/j.biomaterials.2011.04.009 | DOI Listing |
J Colloid Interface Sci
January 2025
Physical Chemistry and Soft Matter, Wageningen University & Research, Stippeneng 4 6708 WE Wageningen, The Netherlands. Electronic address:
Unwanted nonspecific adsorption caused by biomolecules influences the lifetime of biomedical devices and the sensing performance of biosensors. Previously, we have designed B-M-E triblock proteins that rapidly assemble on inorganic surfaces (gold and silica) and render those surfaces antifouling. The B-M-E triblock proteins have a surface-binding domain B, a multimerization domain M and an antifouling domain E.
View Article and Find Full Text PDFChembiochem
January 2025
National Glycoengineering Research Center, Shandong Provincial Key Laboratory of Glycochemistry and Glycobiology, Shandong University, Qingdao, Shandong, 266237, P. R China.
Nucleotide sugars (NSs) are essential building blocks for the enzymatic assembly of glycans. In this study, we established a preparation and recycling avenue to the biocatalysts for the enzymatic synthesis of NSs. This approach involves fusing two enzymes into a bifunctional chimera and using elastin-like polypeptides (ET64) as a purification tag, which allows for easy recovery of these biocatalysts without the need for chromatography.
View Article and Find Full Text PDFActa Biomater
January 2025
Division of Chemical Biology and Medicinal Chemistry, College of Pharmacy, University of Texas at Austin, Austin, TX 78712, USA. Electronic address:
The design of biomaterials that can reconfigure on-demand in response to external stimuli is an emerging area in materials research. However, achieving reversible assembly of protein-based biomaterials by light input remains a major challenge. Here, we present the engineering of a new protein material that is capable of switching between liquid and solid state reversibly, controlled by lights of different wavelengths.
View Article and Find Full Text PDFDrug Deliv
December 2025
Biomedical Materials and Devices for Revolutionary Integrative Systems Engineering (BMD-RISE) Research Unit, Faculty of Engineering, Chulalongkorn University, Bangkok, Thailand.
Biopolymers, such as collagens, elastin, silk fibroin, spider silk, fibrin, keratin, and resilin have gained significant interest for their potential biomedical applications due to their biocompatibility, biodegradability, and mechanical properties. This review focuses on the design and integration of biomimetic peptides into these biopolymer platforms to control the release of bioactive molecules, thereby enhancing their functionality for drug delivery, tissue engineering, and regenerative medicine. Elastin-like polypeptides (ELPs) and silk fibroin repeats, for example, demonstrate how engineered peptides can mimic natural protein domains to modulate material properties and drug release profiles.
View Article and Find Full Text PDFLangmuir
January 2025
Department of Chemistry, University of Washington, Seattle, Washington 98195, United States.
Circular dichroism (CD) spectroscopy has emerged as a potent tool for probing chiral small-molecule ligand exchange on natively achiral quantum dots (QDs). In this study, we report a novel approach to identifying QD-biomolecule interactions by inducing chirality in CdS QDs using thermoresponsive elastin-like polypeptides (ELPs) engineered with C-terminal cysteine residues. Our method is based on a versatile two-step ligand exchange process starting from monodisperse oleate-capped QDs in nonpolar media and proceeding through an easily accessed achiral glycine-capped QD intermediate.
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