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As a novel class of chiral stationary phase (CPS) material, chiral covalent organic frameworks (CCOFs) have already shown great promise in open-tubular capillary electrochromatography (OT-CEC) for chiral separation. The synthesis methods of CCOFs used in OT-CEC mainly include bottom-up, post modification and chiral induction. The CCOFs synthesized by bottom-up and post modification strategies already have lots of applications in capillary electrochromatography, however, the chiral-induced synthesized via an asymmetric catalytic strategy has not yet been reported for using as the chiral stationary phase (CPS) in OT-CEC or even in chromatographic separation. Herein, the chiral-induced COF (Λ)-TpPa-1 was synthesized by asymmetric catalytic synthesis and coated on the inner surface of a capillary by an in-situ growth strategy as the CPS for chiral drug separation. The baseline separation of six enantiomers was achieved within 14 min, with a high-resolution (Rs) range from 1.85 to 6.75. Moreover, the resolution and migration time of the capillary keep stable within 160 runs, showing its superior stability and repeatability. This research provides a new idea for the development and application of novel CPS materials in the field of capillary electrochromatography separation, also shows the new application of chiral induced COFs. Furthermore, the chiral-induced CCOFs can be easily applied to other chromatographic separation fields, exhibiting its extensive application value in chiral analysis separation.

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Collagen, a widely used biomaterial, is susceptible to denaturation during production from native tissues, posing serious challenges for its applications in tissue engineering. Accurate quantification of denatured collagen (DC) is essential for evaluating the quality of collagen-based biomaterials, yet quantitative methods for assessing collagen denaturation are lacking. Here, we for the first time present a highly specific biochip for sensitive quantification of denatured collagen levels (Ldc), addressing this critical need in collagen quality analysis. The denatured collagen-specific chip (DCSC) features an intrinsically nontrimerizing peptide probe, F-GOP-14, targeting denatured collagen and a fully denatured collagen-coated capture surface. The DCSC demonstrates exceptional sensitivity and accuracy in quantifying DC concentration (Cdc) and total collagen concentration (Ctc), enabling precise calculation of Ldc. Importantly, DCSC is versatile, detecting Ldc across various denaturing scenarios, including UV radiation, thermal environments, and decellularization. This denatured collagen-specific biochip offers a robust method for accurately analyzing Ldc, with significant potential for enhancing collagen quality assessment in biomaterial development and production.

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Skin aging, a complex physiological process characterized by alterations in skin structure and function, seriously affects human life. Collagen holds considerable potential in aging skin treatment, while animal-derived collagen poses risks of pathogen transmission. Self-assembled peptides have garnered increasing attention in creating collagen mimetic materials; however, previous reported self-assembled peptides rely on vulnerable non-covalent interactions or lack the capability of controlling morphology and incorporating functional motifs, limiting their ability to mimic collagen structure and function. We have herein created a controllable tyrosine-rich triblock peptide system capable of self-assembling into robust collagen mimetic bioscaffolds for rejuvenating aging skin. Through ruthenium-mediated crosslinking, these peptides self-assemble into well-defined nanospheres or collagen-mimetic scaffolds, precisely regulated by the triple-helical structure and tyrosine distribution. The self-assembled collagen mimetic scaffolds exhibit outstanding resistances to various solvents and pH conditions. The integrin-binding motif has been incorporated into the triple helical block without disrupting their assembly, while endowing them with superior bioactivities, effectively promoting cell adhesion and proliferation. In vivo studies demonstrated their efficacy in treating photoaging skin by accelerating collagen regeneration and activating fibroblasts. The self-assembled tyrosine-rich triblock peptides represent a versatile system for creating robust collagen mimetic biomaterials, providing great potential in skin rejuvenation and tissue regeneration.

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Skin aging is influenced by both external environmental factors and intrinsic biological mechanisms. Traditional microsphere implants aim to rejuvenate aging skin through collagen regeneration, yet their non-biodegradability and risk of granuloma formation often limit their effectiveness. In this study, we developed novel, injectable, highly bioactive, and degradable collagen-chitosan double-crosslinked composite microspheres for skin rejuvenation. The microspheres demonstrated excellent injectability, requiring an injection force of only 0.9 N, and significant biodegradability, effectively degraded in solutions containing phosphate buffer, type I collagenase, and pepsin. In addition, the microspheres exhibited excellent biocompatibility and bioactivity, significantly promoting the proliferation, adhesion, and migration of human foreskin fibroblast-1 (HFF-1) cells. In a photoaged mouse skin model, the implantation of microspheres significantly enhanced dermal density and skin elasticity while reducing transepidermal water loss. Importantly, the implant promoted the regeneration of collagen fibers. This study suggests that collagen-chitosan double-crosslinked composite microspheres hold significant potential for skin rejuvenation treatments.

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Skin damage caused by excessive UV exposure has gradually become one of the most common skin diseases, leading to desquamation, scab formation, inflammation and even skin cancer. Animal-derived hydrolyzed collagen peptides have been developed to treat UV-damaged skin; however, they have raised severe concerns such as potential viral transmission, random sequences and the lack of a triple helix structure. Nano collagen, a novel type of short collagen, has attracted increasing attention in the mimicking of natural collagen, while its applications in UV-damaged skin treatment remains unexplored. Herein, we have created a series of nano collagens and for the first time studied their capability of accelerating UV-damaged skin healing. Nano collagens, consisting of repetitive (GPO)n triplets and a GFOGER motif, display a stable triple-helical structure, significantly promoting fibroblast adhesion, proliferation, and migration. The repair effects of nano collagens have been investigated using an acute UV-damaged skin mouse model. Combo evaluations indicate that nano collagens contribute to recovering the dermis density and erythema index of UV-damaged skin. Histological analysis further demonstrates their capability of promoting the healing of damaged skin by accelerating re-epithelialization and collagen regeneration. These highly bioactive triple-helical nano collagens present a novel strategy for the treatment of UV-damaged skin, providing promising applications in cosmetics and dermatology.

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Photoaged skin, a consequence of UV radiation-induced collagen degradation, presents a significant challenge for skin rejuvenation. Synthetic polymer microspheres, while offering collagen regeneration potential, carry risks like granulomas. To overcome this, we developed a novel agarose-collagen composite microsphere implant for skin tissue regeneration. Fabricated using an emulsification-crosslinking method, these microspheres exhibited excellent uniformity and sphericity (with a diameter of ~38.5 µm), as well as attractive injectability. In vitro studies demonstrated their superior biocompatibility, promoting cell proliferation, adhesion, and migration. Further assessments revealed favorable biosafety and blood compatibility. In vivo experiments in photoaged mice showed that implantation of these microspheres effectively reduced wrinkles, increased skin density, and improved elasticity by stimulating fibroblast encapsulation and collagen regeneration. These findings highlight the potential of agarose-collagen microspheres in dermatological and tissue engineering applications, offering a safer alternative for skin rejuvenation.

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Skin aging, characterized by reduced regeneration, chronic inflammation, and heightened skin cancer risk, poses a significant challenge. Collagen fillers have emerged as a potential solution for skin rejuvenation by stimulating collagen regeneration. However, their clinical efficacy is limited by inherent instability and vulnerability toin vivodegradation by collagenase. Chemical cross-linking presents a promising approach to enhance stability, but it carries risks such as cytotoxicity, calcification, and discoloration. Here, we introduce a highly durable 1,4-butanediol diglycidyl ether (BDDE) cross-linked collagen filler for skin rejuvenation. BDDE effectively cross-links collagen, resulting in fillers with exceptional mechanical strength and injectability. These fillers demonstrate favorable stability and durability, promoting proliferation, adhesion, and spreading of human foreskin fibroblast-1 cellsin vitro. In vivostudies confirm enhanced collagen regeneration without inducing calcification. BDDE cross-linked collagen fillers offer promising prospects for medical cosmetology and tissue regeneration.

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Osteoarthritis (OA), characterized by chronic inflammation and cartilage degeneration, significantly affects over 500 million people globally. Nanoparticles have emerged as promising treatments for OA; however, current strategies often employ a single type of nanoparticle targeting specific disease stages, limiting sustained therapeutic efficacy. In this study, a novel collagen hydrogel is introduced, thiol crosslinked collagen-cerium oxide-poly(D,L-lactic-co-glycolic acid) microspheres encapsulating nanoparticles (CSH-CeO2-pFe2O3), designed for the controlled release of cerium oxide (CeO2) and ferric oxide (Fe2O3) nanoparticles for comprehensive OA management. The sulfhydryl cross-linked collagen matrix embeds CeO2 nanoparticles and poly(D,L-lactic-co-glycolic acid) (PLGA) microspheres encapsulating Fe2O3 nanoparticles. The CSH-CeO2-pFe2O3 hydrogel exhibits enhanced mechanical strength and remarkable injectability, along with a significant promotion of cell adhesion, proliferation, and chondrogenic differentiation. Notably, the hydrogel demonstrates intelligent responsiveness to high levels of reactive oxygen species, initiating the rapid release of CeO2 nanoparticles to address the intense inflammatory responses of early-stage OA, followed by the sustained release of Fe2O3 nanoparticles to facilitate cartilage regeneration during the proliferative phase. In a rat model with cartilage defects, the hydrogel significantly alleviates inflammation and enhances cartilage regeneration, holding substantial potential for effectively managing the pathologically complex OA.

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Skin damage caused by excessive UV radiation has gradually become one of the most prevalent skin diseases. Collagen has gradually found applications in the treatment of UV-damaged skin; however, their high molecular weight greatly limits their capacity to permeate the skin barrier and repair the damaged skin. Nano collagen has garnered growing attentions in the mimicking of collagen; while the investigation of its skin permeability and wound-healing capability remains vacancies. Herein, we have for the first time created a highly biocompatible and bioactive transdermal nano collagen demonstrating remarkable transdermal capacity and repair efficacy for UV-damaged skin. The transdermal nano collagen exhibited a stable triple-helix structure, effectively promoting the adhesion and proliferation of fibroblasts. Notably, the transdermal nano collagen displayed exceptional penetration capabilities, permeating fibroblast and healthy skin. Combo evaluations revealed that the transdermal nano collagen contributed to recovering the intensity and TEWL values of UV-damaged skin to normal level. Histological analysis further indicated that transdermal nano collagen significantly accelerated the repair of damaged skin by promoting the collagen regeneration and fibroblasts activation. This highly biocompatible and bioactive transdermal nano collagen provides a novel substituted strategy for the transdermal absorption of collagen, indicating great potential applications in cosmetics and dermatology.

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The construction of peptides to mimic heterogeneous proteins such as type I collagen plays a pivotal role in deciphering their function and pathogenesis. However, progress in the field has been severely hampered by the lack of capability to create stable heterotrimers with desired functional sequences and without the effect of homotrimers. We have herein developed a set of triblock peptides that can assemble into collagen mimetic heterotrimers with desired amino acids and are free from the interference of homotrimers. The triblock peptides comprise a central collagen-like block and two oppositely charged N-/C-terminal blocks, which display inherent incompetency of homotrimer formation. The favorable electrostatic attraction between two paired triblock peptides with complementary terminal charged sequences promptly leads to stable heterotrimers with controlled chain composition. The independence of the collagen-like block from the two terminal blocks endows this system with the adaptability to incorporate desired amino acid sequences while maintaining the heterotrimer structure. The triblock peptides provide a versatile and robust tool to mimic the composition and function of heterotrimer collagen and may have great potential in the design of innovative peptides mimicking heterogeneous proteins.

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Hepatic fibrosis, the insidious progression of chronic liver scarring leading to life-threatening cirrhosis and hepatocellular carcinoma, necessitates the urgent development of noninvasive and precise diagnostic methodologies. Denatured collagen emerges as a critical biomarker in the pathogenesis of hepatic fibrosis. Herein, we have for the first time developed 3D-printed collagen capture chips for highly specific surface-enhanced Raman scattering (SERS) detection of denatured type I and type IV collagen in blood, facilitating the early diagnosis of hepatic fibrosis. Employing a novel blend of denatured collagen-targeting peptide-modified silver nanoparticle probes (Ag@DCTP) and polyethylene glycol diacrylate (PEGDA), we engineered a robust ink for the 3D fabrication of these collagen capture chips. The chips are further equipped with specialized SERS peptide probes, Ag@ICTP@R1 (S-I) and Ag@IVCTP@R2 (S-IV), tailored for the targeted detection of type I and IV collagen, respectively. The SERS chip platform demonstrated exceptional specificity and sensitivity in capturing and detecting denatured type I and IV collagen, achieving detection limits of 3.5 ng/mL for type I and 3.2 ng/mL for type IV collagen within a 10-400 ng/mL range. When tested on serum samples from hepatic fibrosis mouse models across a spectrum of fibrosis stages (S0-S4), the chips consistently measured denatured type I collagen and detected a progressive increase in type IV collagen concentration, which correlated with the severity of fibrosis. This novel strategy establishes a benchmark for the multiplexed detection of collagen biomarkers, enhancing our capacity to assess the stages of hepatic fibrosis.

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Fly ash derived from municipal solid waste incinerators (MSWIs) harbors significant quantities of heavy metals with high leaching toxicity, resulting in detrimental environmental effects. Pb2+ in fly ash is the ion most likely to exceed permissible levels. However, chemical stabilization methods demonstrate poor efficacy in stabilizing Pb2+ under acidic conditions. Herein, we have developed a robust acid-resistant chelating polymer (25DTF) for enhanced stabilization of Pb2+ in fly ash. 25DTF was synthesized through the reaction of formaldehyde with 2,5-dithiourea. 25DTF exhibited remarkable chelation efficiency, nearing 100%, for Pb2+ in fly ash. 25DTF demonstrated exceptional chelation efficiency, surpassing 99.9%, when interacting with Pb2+ in fly ash at pH ≤ 7. Even under acidic conditions, 25DTF effectively prevented the secondary dissolution of Pb2+. Additionally, it indicated outstanding Pb2+ chelation efficiency across diverse regions of China. The 25DTF chelating agent shows considerable potential in alleviating metal ion contamination in soil, wastewater, and urban environmental management, thereby fostering advancements in environmental stewardship.

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Type IV collagen, a principal constituent of basement membranes, consists of six distinct α chains that assemble into both ABC and AAB-type heterotrimers. While collagen-like peptides have been investigated for heterotrimer formation, the construction of ABC-type heterotrimeric collagen mimetic peptides remains a formidable challenge, primarily due to the intricate composition and arrangement of the chains. We have herein for the first time reported the development of a versatile triblock peptide system to mimic ABC-type heterotrimeric collagen stabilized by salt bridges. The triblock peptides A, B, and C incorporate functional natural type IV collagen sequences in the center, along with charged amino acids at their N and C-terminals. By leveraging electrostatic repulsion at these charged termini, the formation of homotrimers is effectively inhibited, while stable ABC-type heterotrimers are generated through the establishment of salt bridges between oppositely charged terminals. Circular dichroism (CD) spectroscopy demonstrated that peptides A, B, and C existed as individual monomers, while they effectively formed stable ABC-type heterotrimers upon being mixed at a molar ratio of 1:1:1. Additionally, fluorescence quenching results indicated that fluorescence-labeled peptides A', B', and C' formed ABC-type heterotrimer, exhibiting comparable thermal stability as determined by CD spectroscopy. Molecular dynamics simulations elucidated the role of salt bridges between arginine and aspartic acid residues at N- and C-terminals in maintaining a unique chain register in the ABC-type heterotrimers. These triblock peptides offer a robust approach for replicating the structural and functional characteristics of type IV collagen, with promising applications in elucidating the biological roles and pathologies associated with heterotrimeric collagen.

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Skin aging, a complex and inevitable biological process, results in wrinkles, dermal laxity, and skin cancer, profoundly influencing appearance and overall health. Collagen serves as the fundamental element of the dermal matrix; nevertheless, collagen is susceptible to enzymatic degradation within the body. Crosslinking is employed to enhance the physicochemical properties of collagen. However, conventional crosslinking agents may harbor potential issues such as cytotoxicity and calcification risks, constraining their application in the biomedical field. Therefore, we have for the first time developed a highly biocompatible CE-crosslinked collagen implant with exceptional anti-calcification and collagen regeneration capabilities for aging skin rejuvenation. A novel collagen crosslinking agent (CE) was synthesized through a reaction involving chitosan quaternary ammonium salt with 1,4-butanediol diglycidyl ether. Compared to collagen crosslinked with glutaraldehyde (GA), the CE-crosslinked collagen implant exhibited notable stability and durability. The implant demonstrated excellent injectability and viscosity, resisting displacement after implantation. Additionally, the CE-crosslinked collagen implant displayed superior biocompatibility, effectively promoting the proliferation and adhesion of HFF-1 cells compared with the GA-crosslinked collagen. The CE-crosslinked collagen represented a safer and more biologically active implant material. In vivo experiments further substantiated that the implant significantly facilitated collagen regeneration without inducing calcification. The innovative collagen implant has made substantial strides in enhancing aesthetics and reducing wrinkles, presenting the potential for revolutionary progress in the fields of skin rejuvenation and collagen regeneration.

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Skin aging, a complex physiological progression marked by collagen degradation, poses substantial challenges in dermatology. Recombinant collagen emerges as a potential option for skin revitalization, yet its application is constrained by difficulties in forming hydrogels. We have for the first time developed a highly bioactive Tetrakis(hydroxymethyl) phosphonium chloride (THPC)-crosslinked recombinant collagen hydrogel implant for aging skin rejuvenation. THPC demonstrated superior crosslinking efficiency compared to traditional agents such as EDC/NHS and BDDE, achieving complete recombinant collagen crosslinking at minimal concentrations and effectively inducing hydrogel formation. THPC's four reactive hydroxymethyl groups facilitate robust crosslinking with triple helical recombinant collagen, producing hydrogels with enhanced mechanical strength, excellent injectability, increased stability, and greater durability. Moreover, the hydrogel exhibited remarkable biocompatibility and bioactivity, significantly promoting the proliferation, adhesion, and migration of human foreskin fibroblast-1. In photoaged mice skin models, the THPC-crosslinked collagen hydrogel implant notably improved dermal density, skin elasticity, and reduced transepidermal water loss, creating a conducive environment for fibroblast activity and healthy collagen regeneration. Additionally, it elevated superoxide dismutase (SOD) activity and displayed substantial anti-calcification properties. The THPC-crosslinked recombinant collagen hydrogel implant presents an innovative methodology in combating skin aging, offering significant promise in dermatology and tissue engineering.

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The self-assembly of collagen within the human body creates a complex 3D fibrous network, providing structural integrity and mechanical strength to connective tissues. Recombinant collagen plays a pivotal role in the realm of biomimetic natural collagen. However, almost all of the reported recombinant collagens lack the capability of self-assembly, severely hindering their application in tissue engineering and regenerative medicine. Herein, we have for the first time constructed a series of self-assembling tyrosine-rich triple helix recombinant collagens, mimicking the structure and functionality of natural collagen. The recombinant collagen consists of a central triple-helical domain characterized by the (Gly-Xaa-Yaa)n sequence, along with N-terminal and C-terminal domains featuring the GYY sequence. The introduction of GYY has a negligible impact on the stability of the triple-helical structure of recombinant collagen while simultaneously promoting its self-assembly into fibers. In the presence of [Ru(bpy)3]Cl2 and APS as catalysts, tyrosine residues in the recombinant collagen undergo covalent cross-linking, resulting in a hydrogel with exceptional mechanical properties. The recombinant collagen hydrogel exhibits outstanding biocompatibility and bioactivity, significantly enhancing the proliferation, adhesion, migration, and differentiation of HFF-1 cells. This innovative self-assembled triple-helix recombinant collagen demonstrates significant potential in the fields of tissue engineering and medical materials.

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The construction of collagen mimetic peptides has been a hot topic in tissue engineering due to their attractive advantages, such as virus-free nature and low immunogenicity. However, all of the reported self-assembled peptides rely on the inclusion of risky elements of potential safety concerns or lack the capability of incorporating critical functional motifs. A versatile self-assembly design of pure synthetic peptides that can mimic the collagen structure and function remains an insurmountably challenging target. We have herein created a type of triblock peptide consisting of a central triple helical block and N-terminal/C-terminal blocks with oppositely charged amino acids. Favorable electrostatic interactions between the two terminal blocks have been demonstrated to trigger the triblock peptides to form collagen-like nanofibers with a distinct D-banding pattern. A length of 3 or above charged amino acid pairs as well as the maintenance of the triple helical conformation are required for the self-assembly of triblock peptides. Notably, integrin and discoidin domain receptor (DDR) binding sequences GFOGER and GVMGFO have been well demonstrated as vivid examples of convenient incorporation of functional motifs into the triblock peptides without interfering with their self-assembly. These triblock peptides provide a robust and versatile strategy to create next-generation peptide-based biomaterials that can recapitulate the structure and function of collagen, which have promising applications in the fields of tissue engineering and regenerative medicine.

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The accurate detection of multiplex collagen biomarkers is vital for diagnosing and treating various critical diseases such as tumors and fibrosis. Despite the attractive optical properties of quantum dots (QDs), it remains technically challenging to create stable and specific QDs-based probes for multiplex biological imaging. We report for the first time the construction of multi-color QDs-based peptide probes for the simultaneous fingerprinting of multiplex collagen biomarkers in connective tissues. A bipeptide system composed of a glutathione (GSH) host peptide and a collagen-targeting guest peptide (CTP) has been developed, yielding CTP-QDs probes that exhibit exceptional luminescence stability when exposed to ultraviolet irradiation and mildly acidic conditions. The versatile bipeptide system allows for facile one-pot synthesis of high-quality multicolor CTP-QDs probes, exhibiting superior selectivity in targeting critical collagen biomarkers including denatured collagen, type I collagen, type II collagen, and type IV collagen. The multicolor CTP-QDs probes have demonstrated remarkable efficacy in simultaneously fingerprinting multiple collagen types in diverse connective tissues, irrespective of their status, whether affected by injury, diseases, or undergoing remodeling processes. The innovative multicolor CTP-QDs probes offer a robust toolkit for the multiplex fingerprinting of the collagen suprafamily, demonstrating significant potential in the diagnosis and treatment of collagen-related diseases.

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The development of efficacious bone substitute biomaterials remains a major challenge for research and clinical surgical. Herein, we constructed triple helix recombinant collagen (THRC) -based hydrogels loading bone morphogenetic protein-2 (BMP-2) to stimulate bone regeneration in cranial defects. A series of in situ forming hydrogels, denoted as THRC-oxidized carboxymethylcellulose (OCMC)-N-succinyl-chitosan (NSC) hydrogels, was synthesized via a Schiff base reaction involving OCMC, THRC and NSC. The hydrogels underwent rapid formation under physiological pH and temperature conditions. The composite hydrogel exhibits a network structure characterized by uniform pores, the dimensions of which can be tuned by varying THRC concentrations. The THRC-OCMC-NSC and THRC-OCMC-NSC-BMP2 hydrogels display heightened mechanical strength, substantial biodegradability, and lower swelling properties. The THRC-OCMC-NSC hydrogels show exceptional biocompatibility and bioactivity, accelerating cell proliferation, adhesion, and differentiation. Magnetic resonance imaging, computed tomography and histological analysis of rat cranial defects models revealed that the THRC-OCMC-NSC-BMP2 hydrogels substantially promote new bone formation and expedite bone regeneration. The novel THRC-OCMC-NSC-BMP2 hydrogels emerge as promising candidates for bone substitutes, demonstrating substantial potential in bone repair and regeneration applications.

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Full-thickness wounds are severe cutaneous damages with destroyed self-healing function, which need efficient clinical interventions. Inspired by the hierarchical structure of natural skin, we have for the first time developed a biomimetic tri-layered artificial skin (TLAS) comprising silica gel-collagen membrane-collagen porous scaffold for enhanced full-thickness wound healing. The TLAS with the thickness of 3-7 mm displays a hierarchical nanostructure consisting of the top homogeneous silica gel film, the middle compact collagen membrane, and the bottom porous collagen scaffold, exquisitely mimicking the epidermis, basement membrane and dermis of natural skin, respectively. The 1-(3-Dimethylaminopropyl)-3-ethylcarbodiimide/N-Hydroxysuccinimide-dehydrothermal (EDC/NHS-DHT) dual-crosslinked collagen composite bilayer, with a crosslinking degree of 79.5 %, displays remarkable biocompatibility, bioactivity, and biosafety with no risk of hemolysis and pyrogen reactions. Notably, the extra collagen membrane layer provides a robust barrier to block the penetration of silica gel into the collagen porous scaffold, leading to the TLAS with enhanced biocompatibility and bioactivity. The full-thickness wound rat model studies have indicated the TLAS significantly facilitates the regeneration of full-thickness defects by accelerating re-epithelization, collagen deposition and migration of skin appendages. The highly biocompatible and bioactive tri-layered artificial skin provides an improved treatment for full-thickness wounds, which has great potential in tissue engineering.

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