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collagen (Gelfix / Biopad / Condress)

✓ Approved

Merck & Co. · 治疗药物

什么是 collagen？

collagen 是一种治疗药物，由Merck & Co.研发。该药已获批，用于治疗相关适应症，给药途径：Topical。

药物档案

商品名Gelfix, Biopad, Condress
公司Merck & Co.
给药途径Topical
状态Approved
来源： ClinicalTrials.gov, Merck & Co.

治疗适应症

collagen 针对 4 个适应症，涉及 3 个治疗领域。

治疗领域疾病/病症分期
General disorders and administration site conditionsImpaired healing✓ Approved
Skin and subcutaneous tissue disordersDiabetic foot✓ Approved
Skin and subcutaneous tissue disordersDecubitus ulcer✓ Approved
Vascular disordersPeripheral venous disease✓ Approved

相关研究文献

PubMedThe journal of physical chemistry. B2026-09-10

Theoretical Insights into Chlorhexidine Adsorption on Polycaprolactone and Collagen Based Fibers.

Ivankova Yulia I YI, Klimchuk Darya O DO, Sorokin Pavel B PB, Antipina Liubov Yu LY

The interaction of chlorhexidine (CHX) with polycaprolactone (PCL), carboxylated PCL (PCL-COOH), and collagen-containing composite fibers was investigated using density functional tight-binding calculations (DFTB+) to elucidate the mechanisms regulating the immobilization of drugs in antibacterial polymer biomaterials. This work provides an atomistic comparison of adsorption and absorption mechanisms of chlorhexidine in pristine and functionalized PCL matrices and in collagen-PCL composite fibers. On pristine PCL, CHX exhibits moderate adsorption (-0.54 eV), while carboxylic functionalization significantly enhances binding (-1.10 eV) due to hydrogen bonding and increased electronic polarization. At the same time, the higher cohesive stability of the PCL-COOH matrix makes bulk incorporation of CHX energetically unprofitable, limiting sorption mainly by surface adsorption. In contrast, pristine PCL allows both surface adsorption and limited bulk absorption. Modeling of collagen and collagen-PCL composite fibers shows that collagen provides strong binding sites for CHX (-1.06 eV), comparable to those of PCL-COOH and stronger than those of pristine PCL. Frontier orbital analysis and charge density redistribution indicate donor-acceptor interactions in which CHX acts as an electron donor while the collagen matrix serves as the main electron-accepting component. These results suggest that collagen-rich surfaces in composite fibers may provide an effective strategy for immobilizing antibacterial agents in wound-dressing materials.

PMID 42720360
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PubMedImmunological investigations2026-09-10

Toll-Like Receptor 3 Inhibition Reduces Vasoconstriction and Blood Pressure in Spontaneously Hypertensive Rats via COX-1 Downregulation.

Santos Santana Taynara T, Dela Justina Vanessa V, Alves de Freitas Raiany R, Pedrosa Nunes Kenia K et al.

Toll-like receptors (TLRs) are implicated in blood pressure (BP) regulation, but the role of TLR3 in hypertension remains poorly understood. We hypothesized that anti-TLR3 treatment reduces vasoconstriction and lowers BP in hypertension. To test this, spontaneously hypertensive rats (SHR) and normotensive Wistar controls were treated with either IgG or an anti-TLR3 antibody. BP was measured, and mesenteric arteries were assessed for vascular reactivity, protein expression, and histology. Anti-TLR3 treatment significantly reduced BP in SHR. It also decreased the contractile response to noradrenaline, an effect abolished by indomethacin, and prevented the increased COX-1 expression in SHR while reducing COX-2 expression in both strains. Furthermore, anti-TLR3 reduced collagen I and increased collagen III deposition in the mesenteric artery and lowered TLR3 expression in the tunica media of SHR. These findings support TLR3 may represent a novel therapeutic target in hypertension.

PMID 42717682
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PubMedChemistry & biodiversity2026-09-10

Osteogenic Activity of New Dammarane-Type Saponins From Gynostemma pentaphyllum.

Duong Nguyen Tuan NT, Ha Tran Thi Thu TTT, Yen Duong Thi Hai DTH, Thao Do Thi DT et al.

Five dammarane-type saponins (1-5) were isolated from the aerial parts of Gynostemma pentaphyllum, including two new compounds, 2α,3β,12β,19,20(S)-pentahydroxydammar-24-ene 3-O-[β-D-glucopyranosyl-(1→2)-β-D-glucopyranoside]-20-O-[β-D-xylopyranosyl-(1→6)-β-D-glucopyranoside] (1) and 12-oxo-2α,3β,20(S)-trihydroxydammar-24-ene 3-O-(β-D-glucopyranoside)-20-O-[β-D-xylopyranosyl-(1→6)-β-D-glucopyranoside] (2). The structures were elucidated through various spectroscopic analyses (IR, HRESIMS, 1D and 2D NMR). Compounds 1-3 and 5 exhibited osteogenic activity by stimulating alkaline phosphatase (ALP) activity, collagen synthesis, and calcium mineralization in mouse osteoblastic MC3T3-E1 cells. Among these, compound 2 increased ALP activity by 1.30 ± 0.07- and 1.59 ± 0.16-fold at 2 and 1 µg/mL, respectively, whereas compound 1 increased collagen synthesis and calcium mineralization by 1.14 ± 0.05- and 1.24 ± 0.06-fold at 1 µg/mL, and compound 3 increased these parameters by 1.25 ± 0.07- and 1.14 ± 0.03-fold at 2 µg/mL, respectively.

PMID 42720111
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PubMedFrontiers in dental medicine2026-09-10

Phytic acid and grape seed extract in dentin biomodification: effects on bond strength and interface integrity.

Gomes Astrid Ana AA, Devadiga Darshana D, M Roma R, Chandramouli Darshan Madihalli DM et al.

Hybrid layer degradation, driven by residual matrix metalloproteinase (MMP) activity and hydrolytic attack at the resin-dentin interface, remains a primary cause of adhesive restoration failure. Dentin biomodification using natural cross-linking agents represents a promising strategy to enhance collagen stability and inhibit enzymatic degradation of the bonded interface. To evaluate and compare the effect of collagen cross linking agents, phytic acid (IP6) and grape seed extract (GSE), to reinforce the shear bond strength (SBS) of resin composite to dentin. Enamel of 34 human maxillary premolars was eliminated and each tooth was sectioned to make a total sample size of 68 which was divided into four groups (n = 17) for surface treatment: G1-PA:37% Phosphoric acid (control), G2-IP6:1% phytic acid, G3-PA + GSE:37% phosphoric acid+6.5% GSE and G4-IP6 + GSE:1% phytic acid+6.5% GSE. A hybrid resin composite material was bonded and subjected to 1,000 cycles of thermocycling followed by SBS testing and analysis of fracture mode by Scanning Electron Microscopy. The data was statistically analysed using one-way Analysis of Variance (ANOVA) followed by Tukey's Honestly Significant Difference (HSD) post hoc test. G4-IP6 + GSE showed the highest SBS (23.44 ± 4.28 MPa), followed by G2-IP6 (21.51 ± 6.00 MPa) and G3-PA + GSE (21.01 ± 4.35 MPa), while G1-PA had the lowest values of 15.40 ± 4.60 MPa. FTIR analysis showed that phytic acid exhibited a broad peak at 3311.77 cm⁻1 while GSE showed peaks 3266.37 cm⁻1 and 1602.93 cm⁻1 corresponding to hydroxyl and carbonyl functional groups. Phytic acid and grape seed extract significantly improved the composite-dentin shear bond strength of dentin. Their application appears to enhance the structural integrity of demineralized collagen at the resin-dentin interface, thereby supporting their potential incorporation into adhesive restorative protocols as a promising strategy to enhance dentin bond strength.

PMID 42718430
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PubMedAnalytical methods : advancing methods and applications2026-09-10

Development of a multi-technique analytical strategy for the thermal stability assessment of recombinant humanized type III collagen.

Cui Xinling X, Cao Junxia J, Kan Ying Y, Ying Wantao W et al.

To ensure the stability and efficacy of recombinant collagen during development, storage, and application, it is essential to establish systematic and reliable stability assessment methodologies. This study developed and validated an integrated multi-technique analytical strategy for the comprehensive evaluation of the thermal stability of recombinant humanized type III collagen (rhCol III). The strategy combines size exclusion chromatography-multi-angle light scattering (SEC-MALS), dynamic light scattering (DLS), circular dichroism spectroscopy (CD), SDS-PAGE, and µLC-MS/MS to perform correlative analyses of physical aggregation, secondary structure, chemical modifications, and biological functions in samples stored under accelerated degradation conditions (40 °C) and control conditions (4 °C) for three months. The results demonstrate that the established strategy can systematically differentiate and quantify degradation pathways under different temperature conditions. SEC-MALS, SDS-PAGE and DLS revealed that high-temperature storage significantly increased the formation of large aggregates (>100 nm), while circular dichroism spectroscopy confirmed that the secondary structure remained largely intact. The core of the strategy, µLC-MS/MS-based post-translational modification (PTM) analysis, quantitatively elucidated key chemical modifications: oxidation (up to 16.86%) and deamidation (up to 12.31%) levels were markedly elevated, whereas proline-4-hydroxylation, essential for structural stability, was substantially reduced (<6%). Key modification sites (e.g., N425, M131, and P144/P132) were successfully localized and found to be enriched in thermally sensitive regions N- and C-termini. This chemical modification profile was highly consistent with functional assay results: samples stored at 4 °C exhibited significantly superior promotion of cell adhesion (+42% vs. +21%) and migration (45.28% vs. 42.05%) compared to those stored at 40 °C. Moreover, the study found that a higher moisture content in the lyophilized samples not only significantly reduced aggregate formation but also affected the levels of PTMs. The analytical strategy developed in this study enables multidimensional and correlative assessment of protein stability. It not only provides a key stability-indicating methodology for rhCol III but also offers an analytical reference framework for stability studies, process optimization, and quality control of biomacromolecular materials.

PMID 42720449
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PubMedFrontiers in immunology2026-09-10

Secoisolariciresinol diglucoside alleviates inflammatory injury in osteoarthritis chondrocytes through ERBB2-associated JAK2/STAT3 signaling: network pharmacology and experimental validation.

Hu Haibei H, Li Gaoshan G, Wang Yangxu Y, Xie Suyu S et al.

Cartilage injury is a hallmark of osteoarthritis (OA). erb-B2 receptor tyrosine kinase 2 (ERBB2) has been reported to be involved in mediating the therapeutic effects of polyphenols in orthopedic diseases. This study aimed to investigate the protective effects and underlying mechanisms of action of ERBB2 in OA chondrocytes. Bioinformatics analysis and molecular docking were used to predict the binding relationship between ERBB2 and the polyphenolic compound, secoisolariciresinol diglucoside (SDG). ATDC5 cells were induced with insulin-transferrin-selenium (ITS), followed by lipopolysaccharide (LPS) exposure to mimic OA inflammation, and treated with SDG. Cell viability, collagen II expression, apoptosis, interleukin 6 (IL-6)/Tumor Necrosis Factor-α (TNF-α) secretion, and malondialdehyde (MDA)/superoxide dismutase (SOD) levels were evaluated using cell counting kit-8 (CCK-8), immunofluorescence, flow cytometry, enzyme-linked immunosorbent assay (ELISA), and commercial kits. Matrix metalloproteinase 13 (MMP13) and ERBB2 mRNA levels were assessed by quantitative real-time polymerase chain reaction (qRT-PCR). Extracellular matrix integrity was assessed by toluidine blue staining. The predicted SDG-ERBB2 interaction was validated using a cellular thermal shift assay (CETSA). Western blotting was performed to assess the expression of ERBB2 and JAK2/STAT3. Rescue experiments with ERBB2 overexpression or colivelin (a JAK/STAT activator) treatment confirmed the involvement of this pathway. SDG dose-dependently reversed the LPS-induced reduction in cell viability and collagen II expression, while suppressing apoptosis, IL-6/TNF-α secretion, and MDA levels, and increasing SOD activity. SDG significantly reduced MMP13 mRNA levels and enhanced extracellular matrix proteoglycan deposition, indicating the preservation of matrix integrity. ERBB2 has been identified as a candidate target for SDG. SDG inhibits ERBB2 protein expression and reduces JAK2 and STAT3 phosphorylation ERBB2 overexpression and colivelin treatment abrogated the protective effects of SDG on cell viability, collagen II expression, apoptosis, inflammation, and oxidative stress, as well as its suppression of MMP13 and preservation of matrix integrity. SDG protects chondrocytes against LPS-induced inflammatory injury by targeting ERBB2 and suppressing the downstream JAK2/STAT3 signaling pathway. These findings provide mechanistic evidence supporting the chondroprotective potential of SDG under inflammatory conditions and suggest that ERBB2/JAK2/STAT3 signaling may represent a potential therapeutic target in OA.

PMID 42718780
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