3D-Printed SERS Chips for Highly Specific Detection of Denatured Type I and IV Collagens in Blood for Early Hepatic Fibrosis Diagnosis.

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.

A highly biocompatible and bioactive transdermal nano collagen for enhanced healing of UV-damaged skin.

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.

A robust acid-resistant chelating polymer for enhanced stabilization of lead ions in fly ash.

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.

Versatile triblock peptides mimicking ABC-type heterotrimeric collagen with stabilizing salt bridges.

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.

Self-Assembling Triple-Helix Recombinant Collagen Hydrogel Enriched with Tyrosine.

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.

A highly biocompatible CE-crosslinked collagen implant with exceptional anti-calcification and collagen regeneration capabilities for aging skin rejuvenation.

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.

A highly bioactive THPC-crosslinked recombinant collagen hydrogel implant for aging skin rejuvenation.

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.

Simultaneous fingerprinting of multiplex collagen biomarkers in connective tissues by multicolor quantum dots-based peptide probes.

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.

Versatile Triblock Peptide Self-Assembly System to Mimic Collagen Structure and Function.

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.

Bone morphogenetic protein-2 loaded triple helix recombinant collagen-based hydrogels for enhancing bone defect healing.

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.

Biomimetic tri-layered artificial skin comprising silica gel-collagen membrane-collagen porous scaffold for enhanced full-thickness wound healing.

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.

A robust and versatile host-guest peptide toolbox for developing highly stable and specific quantum dot-based peptide probes for imaging extracellular matrices and cells.

Multiplex fluorescence imaging plays a vital role in precision medicine for targeting complex diseases with diverse biomolecular signatures. Quantum dot (QD) probes with vibrant colors are promising candidates for multiplex imaging, but their stability and specificity are frequently compromised by the current tedious post-modification process. We have herein developed a robust and versatile host-guest peptide (HGP) toolbox for creating highly stable and specific QD-based peptide probes for imaging extracellular matrices and cells. The HGP system comprises a host peptide and a guest peptide with a shared sequence pattern of cysteine and negatively charged amino acids, allowing for QD stabilization and specificity towards targeted biomarkers. HGP has been demonstrated as a convenient one-step approach to construct hydrophilic QD-based peptide probes with superior stability under various conditions. Six multicolor HGP-modified QDs have been developed to specifically target extracellular matrix proteins such as collagen, laminin, and nidogen, as well as major cellular elements like the membrane, nucleus, and cytoplasm, providing an efficient tool for real-time monitoring of high-resolution interactions between cancer cells and the extracellular matrix. The HGP system represents a next-generation approach to developing QDs with unprecedented stability and specificity, holding great potential in multiplex imaging and precision medicine.

Ferrous/Ferric Ions Crosslinked Type II Collagen Multifunctional Hydrogel for Advanced Osteoarthritis Treatment.

Osteoarthritis (OA) is a highly prevalent and intricate degenerative joint disease affecting an estimated 500 million individuals worldwide. Collagen-based hydrogels have sparked immense interest in cartilage tissue engineering, but substantial challenges persist in developing biocompatible and robust crosslinking strategies, as well as improving their effectiveness against the multifaceted nature of OA. Herein, a novel discovery wherein the simple incorporation of ferrous/ferric ions enables efficient dynamic crosslinking of type II collagen, leading to the development of injectable, self-healing hydrogels with 3D interconnected porous nanostructures, is unveiled. The ferrous/ferric ions crosslinked type II collagen hydrogels demonstrate exceptional physical properties, such as significantly enhanced mechanical strength, minimal swelling ratios, and remarkable resistance to degradation, while also exhibiting extraordinary biocompatibility and bioactivity, effectively promoting cell proliferation, adhesion, and chondrogenic differentiation. Additionally, the hydrogels reveal potent anti-inflammatory effects by upregulating anti-inflammatory cytokines while downregulating pro-inflammatory cytokines. In a rat model of cartilage defects, these hydrogels exhibit impressive efficacy, substantially accelerating cartilage tissue regeneration through enhanced collagen deposition and increased proteoglycan secretion. The innovative discovery of the multifunctional role of ferrous/ferric ions in endowing type II collagen hydrogels with a myriad of beneficial properties presents exciting prospects for developing advanced biomaterials with potential applications in OA.

Recombinant Collagen-Templated Biomineralized Synthesis of Biocompatible pH-Responsive Porous Calcium Carbonate Nanospheres.

The synthesis of calcium carbonate with controlled morphology is crucial for its biomedical applications. In this study, we synthesized well-ordered porous calcium carbonate nanospheres using recombinant collagen as a biomineralization template. Porous collagen-calcium carbonate was created by incubating calcium chloride and sodium carbonate with collagen biotemplates at room temperature. Our results show that the recombinant collagen-calcium carbonate nanomaterials underwent a morphological transition from solid nanospheres to more porous nanospheres and a phase transformation from vaterite to a mixture of calcite and vaterite. This study highlights the crucial role of recombinant collagen in modulating the morphology and crystallinity of calcium carbonate nanoparticles. Importantly, the highly porous recombinant collagen-calcium carbonate hybrid nanospheres demonstrated superior loading efficacy for the model drug cefoperazone. Furthermore, the drug loading and releasing results suggest that hybrid nanospheres have the potential to be robust and biocompatible pH-responsive drug carriers. Our findings suggest that recombinant collagen's unique amino acid content and rodlike structure make it a superior template for biomineralized synthesis. This study provides a promising avenue for the production of novel organic-inorganic nanostructures, with potential applications in biomedical fields such as drug delivery.

Biocompatible and bioactive hydrogels of recombinant fusion elastin with low transition temperature for improved healing of UV-irradiated skin.

Prolonged exposure to UV radiation can cause severe photodamage to the skin, leading to abnormal fragmentation of elastin fibers. As one of the main protein components of the dermal extracellular matrix, elastin plays a critical role in the mechanical behavior and physiological function of the skin. Animal-derived elastin has attracted extensive attention in tissue engineering, however it suffers from severe drawbacks such as a risk of virus transmission, ready degradation, and challenging quality control. Herein, we have for the first time developed a novel recombinant fusion elastin (RFE) and its cross-linked hydrogel for improved healing efficacy for UV-irradiated skin. RFE showed temperature-sensitive aggregation behavior similar to natural elastin. Compared with recombinant elastin without the fusion V-foldon domain, RFE showed a much more ordered secondary structure and lower transition temperature. Furthermore, Native-PAGE results indicated that the addition of the V-foldon domain triggered the formation of remarkable oligomers in RFE, which may result in a more ordered conformation. Tetrakis Hydroxymethyl Phosphonium Chloride (THPC) cross-linking of RFE led to the production of a fibrous hydrogel with uniform three-dimensional porous nanostructures and excellent mechanical strength. The RFE hydrogel showed superior cellular activity, significantly promoting the survival and proliferation of human foreskin fibroblast-1 (HFF-1). Studies of mice models of UV-irradiated skin demonstrated that the RFE hydrogel pronouncedly accelerated their healing process by inhibiting epidermal hyperplasia as well as boosting the regeneration of collagen and elastin fibers. The highly biocompatible and bioactive recombinant fusion elastin and its cross-linked hydrogel provide a potent treatment for photodamaged skin, which may have promising applications in dermatology and tissue engineering.

Peptide-triggered self-assembly of collagen mimetic peptides into nanospheres by electrostatic interaction and π-π stacking.

Collagen is the most abundant protein in various connective tissues, providing mechanical integrity as well as regulating cellular activities. Self-assembled peptides have been extensively explored to develop collagen mimetic materials, due to their attractive features such as easy synthesis, selective sequences and low immunogenicity. Metal ion-triggered self-assembly of collagen mimetic peptides has recently received increasing interests, since the addition of external stimuli offers programmable control of the self-assembly process. We have for the first time reported a peptide-stimulated self-assembly of collagen mimetic peptides into nanospheres by electrostatic interaction and π-π stacking. We have accidentally discovered that FAM-modified positively-charged triple helical peptide FAM-PRG was highly soluble, while the addition of a single-stranded negatively-charged peptide EOG-10 efficiently drove its self-assembly into well-ordered spherical nanomaterials. Peptide EOG-10 has been shown to mediate similar self-assembly of TPE-modified triple-helical peptide TPE-PRG into luminescent exquisite nanospheres, consistently demonstrating the robustness of this peptide-triggered strategy. Fluorescence monitoring of the interaction of EOG-10 and TPE-PRG at different ratios indicated that EOG-10 specifically binds to TPE-PRG to form a 3 : 1 complex. High salt concentration was shown to inhibit the self-assembly of TPE-PRG with EOG-10, suggesting that their self-assembly was controlled by electrostatic interaction. The self-assembly of TPE-PRG with EOG-10 has been further revealed to require the exact lengths of both peptides as well as complementary sequences without mutations, indicating a pairwise "side-by-side" binding mode. Notably, the identity of the N-terminal residues of X-PRG has been found to play a determinant role in the self-assembly, while non-aromatic residues lost the self-assembling capability, suggesting that π-π stacking and electrostatic interactions collectively modulate the self-assembly of X-PRG and EOG-10. To conclude, we have developed a highly biocompatible and programmably controlled peptide-triggered self-assembly approach to create novel collagen mimetic nanomaterials, which may have great potential in advanced functional materials.

A robust collagen-targeting MRI peptide contrast agent for in vivo imaging of hepatic fibrosis.

We herein report the construction of a robust MRI peptide contrast agent Gd-ICTP with superior selectivity for type I collagen, enabling the accurate and non-invasive detection of hepatic fibrosis in vivo.

Concentration-mediated Folding and Unfolding of Collagen Triple Helix.

BACKGROUND: Collagen has been widely utilized in tissue engineering, regenerative medicine and cosmetics. Collagen of low concentrations is frequently applied to reduce the production cost, while it may result in the loss of triple helical structure and bioactivity. CD and NMR techniques have enhanced our understanding of collagen triple helix, while they require high concentrations of collagen samples. OBJECTIVE: We have systematically investigated the folding and unfolding features of collagen mimetic peptides at a broad variety of concentrations in order to decipher the role of the concentration in the triple helical stability. METHODS: Peptide FAM-G(POG)10 was synthesized by the solid phase synthesis method. Fluorescence spectra of peptide FAM-G(POG)10 at different concentrations were recorded. The unfolding and folding profiles of peptide FAM-G(POG)10 with concentrations varying from 1 nM to 100 µM were examined. The effect of concentration on the folding and unfolding capability of peptide FAMG( POG)10 was investigated. RESULTS: Fluorescence characterization of peptide FAM-G(POG)10 under widely varying concentrations from 1 nM to 100 µM has revealed that concentration played a critical role in the stability of collagen peptides. The two-phase pattern of the concentration-dependent folding and unfolding curves has for the first time demonstrated the presence of a critical concentration for the collagen peptide to trigger the complete folding of the triple helix and to maintain the triple helix structure. It is noteworthy that the triple helix structure of collagen peptides was very stable at µM-level concentrations from both the folding and unfolding perspectives. CONCLUSION: It has significantly contributed to our understanding of collagen triple helix stability at low and ultra-low concentrations, and provided valuable and practical guidelines for the preparation of collagen-based products.

Non-denatured yak type I collagen accelerates sunburned skin healing by stimulating and replenishing dermal collagen.

Sunburn is one of the most common skin lesions caused by excessive UV exposure, and its incidence is highly correlated with the risks of skin cancer. A variety of drugs including corticosteroids and NSAIDs have been developed to treat acute sunburn, however, they have raised severe concerns such as poor healing efficacy and long recovery time. We have for the first time extracted non-denatured type I collagen from yak hide, which displays a canonical triple helical structure with melting temperature of 42.7 °C. The highly pure yak collagen type I (YCI) self-assembles to form well-ordered nanofibers with periodic d-bands. YCI is highly biocompatible, and it significantly promotes the proliferation and adhesion of HFF-1 cells. The sunburn healing effects of YCI has been investigated using acute skin injury mouse model. Histological analysis shows that 4 days' treatment of YCI has resulted in the recovery of sunburned mice skin to a healthy state, indicated by pronounced acceleration of epithelization and collagen deposition. The collagen volume fraction as well as the hydroxyproline (Hyp) content of YCI-treated sunburned skin have been found to be greatly increased, confirming the enhanced regeneration of collagen. YCI creams and dressings have also shown superior healing capacity of sunburn by remarkably shortening the recovery time. Notably, the denatured collagen-targeted staining results indicated a large quantity of denatured collagen in sunburned mice, which became substantially reduced after the YCI treatment. FITC-labeled YCI has been further found to penetrate into the dermis of sunburned mice. The highly biocompatible and bioactive non-denatured YCI provides an improved treatment of sunburn, indicating very promising applications of YCI in cosmetics and dermatology.

Apple-like Zinc-Oxide Mesocrystals as Robust and Versatile Photocatalysts for Efficient Degradation of Eight Different Organic Dyes.

The discovery of efficient photocatalysts is a promising key approach to solve the environmental crisis caused by hazardous organic dyes. Herein, we have for the first time created ZnO mesocrystals with a novel apple-like morphology. We have developed a one-pot biomineralization route to synthesize ZnO nanostructures at room temperature by using the rod-like protein collagen as the template. The shape of ZnO mesocrystals can be conveniently tuned from fusiform-like and kiwi-like to orange-like, apple-like, and snack-like structures. The apple-like ZnO mesocrystals show a significantly better photodegradation efficiency than the commercial ZnO powder as well as other nanostructured ZnO materials for both rhodamine B (RhB) and methyl orange (MO). Furthermore, the apple-like zinc-oxide mesocrystals can degrade all of the tested eight different types of organic dyes (RhB, rhodamine 6G, methylene blue, Coomassie brilliant blue R250, BPB, MO, Li Chunhong S, and carmine) simply under the exposure of sunlight, demonstrating their superior photodegradation prowess, environmental amiability, and energy-saving features. The novel robust and versatile photocatalyst has greatly advanced our abilities for the elimination of organic dyes. The green, one-pot strategy provides a convenient method for the construction of novel metal-oxide nanostructures with promising applications in environmental protection.