Biomacromolecules最新文献

{"title":"Secondary Structure of i‑Motif DNA Modulates Phase Separation","authors":"Ushosi Bhattacharyya,&nbsp;Nibedita Pal","doi":"10.1021/acs.biomac.6c01266","DOIUrl":"10.1021/acs.biomac.6c01266","url":null,"abstract":"<div><div>Liquid–liquid phase separation is central to nucleic acid organization in cells, yet the role of DNA secondary structures in phase separation is largely underexplored. Using confocal fluorescence microscopy, we investigated phase separation of i-motif (iM)-forming sequences in the presence of poly-<span> <em>l</em> </span>-lysine under varying pHs. iMs are four-stranded DNA structures formed in cytosine-rich sequences, often enriched in oncogenes and telomeres. At acidic pH, fully folded iMs suppressed droplet formation, indicating that structural stiffness inhibits phase separation. Near the transition pH, partially folded iMs formed gel-like droplets with high contact angles. At basic pH, unfolded iMs exhibited fluid-like droplets with lower contact angles. Disrupting the iM secondary structure via cytosine deamination restored liquid-like droplets at transitional pH, confirming the role of structure. In contrast, stable G-quadruplex structures consistently formed high-contact-angle droplets. These findings highlight the DNA secondary structure as a key determinant of biomolecular condensate formation, morphology, and dynamics, with potential implications for gene expression.</div></div><div>Liquid–liquid phase separation is central to nucleic acid organization in cells, yet the role of DNA secondary structures in phase separation is largely underexplored. Using confocal fluorescence microscopy, we investigated phase separation of i-motif (iM)-forming sequences in the presence of poly-<span> <em>l</em> </span>-lysine under varying pHs. iMs are four-stranded DNA structures formed in cytosine-rich sequences, often enriched in oncogenes and telomeres. At acidic pH, fully folded iMs suppressed droplet formation, indicating that structural stiffness inhibits phase separation. Near the transition pH, partially folded iMs formed gel-like droplets with high contact angles. At basic pH, unfolded iMs exhibited fluid-like droplets with lower contact angles. Disrupting the iM secondary structure via cytosine deamination restored liquid-like droplets at transitional pH, confirming the role of structure. In contrast, stable G-quadruplex structures consistently formed high-contact-angle droplets. These findings highlight the DNA secondary structure as a key determinant of biomolecular condensate formation, morphology, and dynamics, with potential implications for gene expression.</div><div><div><span><figure><span><img><ol><li><span><span>Download: <span>Download high-res image (110KB)</span></span></span></li><li><span><span>Download: <span>Download full-size image</span></span></span></li></ol></span></figure></span></div></div><div><span><figure><span><img><ol><li><span><span>Download: <span>Download high-res image (110KB)</span></span></span></li><li><span><span>Download: <span>Download full-size image</span></span></span></li></ol></span></figure></span></div>","PeriodicalId":30,"journal":{"name":"Biomacromolecules","volume":"27 9","pages":"Pages 6190-6198"},"PeriodicalIF":5.9,"publicationDate":"2026-09-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148958039","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Chain-Folding-Regulated Assembly of an Amphiphilic Glycopolymer with Outstanding Functional Group Display and Multivalent Interactions with Biological Targets","authors":"Soumya Koner,&nbsp;Krishna Dan,&nbsp;Priya Rajdev,&nbsp;Suhrit Ghosh","doi":"10.1021/acs.biomac.6c01170","DOIUrl":"10.1021/acs.biomac.6c01170","url":null,"abstract":"<div><div>This manuscript describes chain-folding-regulated hierarchical self-assembly of an amphiphilic polyurethane (P1), exhibiting superior surface functional group display and biological activity compared to an analogous amphiphilic block copolymer (P3) or a rigid polyurethane (P2) that is deprived of chain folding. In P1, intrachain hydrogen bonding directs the formation of a pleated structure that hierarchically assembles into hollow capsules. A glucose oxidase–peroxidase assay confirmed that this unique assembly of P1 allows displaying ∼50% glucose moieties on the outer surface, which significantly outperforms amphiphilic block copolymers. This renders outstanding multivalent binding with the lectin concanavalin A, as is evident by a very high association constant (∼10⁵ M^–1) and spontaneous glycocluster effect. In contrast, P2 or P3 fails to exhibit any notable glycocluster effect under identical conditions. Furthermore, P1, unlike P2 or P3, induced clustering of Staphylococcus aureus by targeting bacterial carbohydrate transporters, deactivated the bacteria, and prevented internalization into mammalian cells.</div></div><div>This manuscript describes chain-folding-regulated hierarchical self-assembly of an amphiphilic polyurethane (P1), exhibiting superior surface functional group display and biological activity compared to an analogous amphiphilic block copolymer (P3) or a rigid polyurethane (P2) that is deprived of chain folding. In P1, intrachain hydrogen bonding directs the formation of a pleated structure that hierarchically assembles into hollow capsules. A glucose oxidase–peroxidase assay confirmed that this unique assembly of P1 allows displaying ∼50% glucose moieties on the outer surface, which significantly outperforms amphiphilic block copolymers. This renders outstanding multivalent binding with the lectin concanavalin A, as is evident by a very high association constant (∼10⁵ M^–1) and spontaneous glycocluster effect. In contrast, P2 or P3 fails to exhibit any notable glycocluster effect under identical conditions. Furthermore, P1, unlike P2 or P3, induced clustering of Staphylococcus aureus by targeting bacterial carbohydrate transporters, deactivated the bacteria, and prevented internalization into mammalian cells.</div><div><div><span><figure><span><img><ol><li><span><span>Download: <span>Download high-res image (88KB)</span></span></span></li><li><span><span>Download: <span>Download full-size image</span></span></span></li></ol></span></figure></span></div></div><div><span><figure><span><img><ol><li><span><span>Download: <span>Download high-res image (88KB)</span></span></span></li><li><span><span>Download: <span>Download full-size image</span></span></span></li></ol></span></figure></span></div>","PeriodicalId":30,"journal":{"name":"Biomacromolecules","volume":"27 9","pages":"Pages 6156-6164"},"PeriodicalIF":5.9,"publicationDate":"2026-09-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148958038","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Multicomponent Micelles with Boosted Stability of Iminoboronates","authors":"Junfei Hu,&nbsp;Jianhua Zhang,&nbsp;Wenjing Liu,&nbsp;Junmei Song,&nbsp;Tianyou Wang,&nbsp;Junru Tao,&nbsp;Yiwen Li,&nbsp;Zhan Li","doi":"10.1021/acs.biomac.6c01208","DOIUrl":"10.1021/acs.biomac.6c01208","url":null,"abstract":"<div><div>Multicomponent reactions (MCRs) enable efficient construction of multifunctional materials, with iminoboronate chemistry offering attractive pH and redox responsiveness for smart biomaterials. However, their poor kinetic stability under aqueous dilution and elevated CO₂ levels limit biomedical applications. Herein, we address this challenge by embedding iminoboronate linkages within supramolecular assemblies, where nanoconfinement modulates their kinetic behaviors. The hydrophobic microenvironment of the supramolecular micellar core effectively restricts water accessibility to the iminoboronate moieties, converting the inherent kinetic instability into assembly-dependent and environment-regulated stability. By varying amine derivatives and natural polyphenols, a series of multicomponent supramolecular micelles were constructed. In cellular studies and postoperative skin cancer models, multifunctional micelles coloaded with doxorubicin and epigallocatechin gallate exhibited a synergistic therapeutic profile, effectively suppressing tumor recurrence while simultaneously promoting wound healing. This work establishes supramolecular confinement as a general strategy to stabilize kinetically labile MCR-derived linkages, expanding the biomedical potential of iminoboronate chemistry.</div></div><div><div><span><figure><span><img><ol><li><span><span>Download: <span>Download high-res image (213KB)</span></span></span></li><li><span><span>Download: <span>Download full-size image</span></span></span></li></ol></span></figure></span></div></div>","PeriodicalId":30,"journal":{"name":"Biomacromolecules","volume":"27 8","pages":"Pages 5784-5794"},"PeriodicalIF":5.9,"publicationDate":"2026-08-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148381227","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Metal-Ion-Modulated Stabilization of Intermediates in Diphenylalanine and Phenylalanine Self-Assembly: Roles of Metal-Ion-Specific Salt Bridges and Hydrophobic Interactions","authors":"Priyanka Nath,&nbsp;Suman Choudhury,&nbsp;Huma Tabassum,&nbsp;Naveen Kumar,&nbsp;Sheetal Leva,&nbsp;Avijit Maity,&nbsp;Debanjan Bagchi,&nbsp;Suman Das,&nbsp;Anjan Chakraborty","doi":"10.1021/acs.biomac.6c01062","DOIUrl":"10.1021/acs.biomac.6c01062","url":null,"abstract":"<div><div>The self-assembly of aromatic amino acids and short peptides into fibrillar structures involves transient intermediates whose roles remain poorly understood, despite their potential involvement in cytotoxicity and disease progression. Here, we investigate the self-assembly of diphenylalanine (FF) and phenylalanine (Phe) in the presence of biologically relevant divalent metal ions: Ca²⁺, Mg²⁺, and Zn²⁺. These ions significantly influence the assembly pathways by stabilizing distinct intermediate structures and delaying fibril formation, particularly at higher ion concentrations. Notably, FF assemblies form long-lived microspherical structures in the presence of Ca²⁺ and Mg²⁺ without transitioning into fibrils. Molecular dynamics simulations provide a mechanistic interpretation of the experimental observations, from compact aggregates to multicluster states. Ca²⁺ stabilizes FF cluster intermediates through salt-bridge interactions, Mg²⁺ drives aggregation via hydration-mediated effects, and Zn²⁺ acts through a combination of hydrophobic and salt-bridge interactions. These findings reveal the role of metal ions in the phenylalanine-rich dipeptide assembly and their potential as biomimetic materials.</div></div><div><div><span><figure><span><img><ol><li><span><span>Download: <span>Download high-res image (117KB)</span></span></span></li><li><span><span>Download: <span>Download full-size image</span></span></span></li></ol></span></figure></span></div></div>","PeriodicalId":30,"journal":{"name":"Biomacromolecules","volume":"27 8","pages":"Pages 5711-5724"},"PeriodicalIF":5.9,"publicationDate":"2026-08-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148402943","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Ruthenium Dioxide-Incorporated Dual-Responsive Hydrogel Promotes MRSA-Infected Diabetic Wound Healing via Microenvironment Remodeling","authors":"Rongrong Li,&nbsp;Shangbo Zhang,&nbsp;Zan Wang,&nbsp;Junlei He,&nbsp;Yue Zhao,&nbsp;Yongchao Liu,&nbsp;Liyuan Sun,&nbsp;Jianbin Li,&nbsp;Jiahao Liu,&nbsp;Tianshun Zhang,&nbsp;Shidong Zhang,&nbsp;Ting Liu,&nbsp;Jianxi Song","doi":"10.1021/acs.biomac.6c00727","DOIUrl":"10.1021/acs.biomac.6c00727","url":null,"abstract":"<div><div>Severe microenvironmental imbalance in diabetic wounds infected with drug-resistant bacteria, a clinically prevalent issue yet often overlooked as a distinct pathological entity, results in a lack of coordinated multidimensional regulation of the wound microenvironment, which remains largely underexplored in current studies. Herein, we report a pH/ROS-responsive multifunctional hydrogel (G@Ru) incorporating RuNPs. G@Ru is constructed via dynamic Schiff base and boronate ester linkages, which endow it with dual stimulus responsiveness, injectability, adhesiveness, self-healing, and hemostatic properties. In addition, the intrinsic antibacterial activity of RuNPs enables the inhibition of methicillin-resistant Staphylococcus aureus. Furthermore, in vivo studies confirm that G@Ru can regulate macrophage polarization, modulate reactive oxygen species levels, enhance cell proliferation, stimulate angiogenesis, and accelerate tissue regeneration, thereby reshaping the wound microenvironment in a multidimensional manner. Ultimately, G@Ru exhibits superior therapeutic efficacy, achieving a wound closure rate of 98% in infected diabetic wounds by day 14, highlighting its antibiotic-free therapeutic potential and promising clinical translational applications.</div></div><div><div><span><figure><span><img><ol><li><span><span>Download: <span>Download high-res image (103KB)</span></span></span></li><li><span><span>Download: <span>Download full-size image</span></span></span></li></ol></span></figure></span></div></div>","PeriodicalId":30,"journal":{"name":"Biomacromolecules","volume":"27 8","pages":"Pages 5432-5448"},"PeriodicalIF":5.9,"publicationDate":"2026-08-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148547029","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Nonuniform Curvature and Bending Rigidity of Adsorbed Collagen Molecules in Aqueous Solution","authors":"Daniela A. Barragàn Rivera,&nbsp;Maria P. De Santo,&nbsp;Elvira Brunelli,&nbsp;Pierluigi Bilotto,&nbsp;Philipp J. Thurner,&nbsp;Guido Raos,&nbsp;Bruno Zappone","doi":"10.1021/acs.biomac.6c00845","DOIUrl":"10.1021/acs.biomac.6c00845","url":null,"abstract":"<div><div>Collagen, the most abundant protein in mammals, plays a key role in tissue formation and mechanics due to its triple-helix structure. We used atomic force microscopy to study individual type-I and type-III human collagen molecules adsorbed on smooth mica surfaces from low-salt, near-neutral aqueous solutions. Statistical analysis of their two-dimensional contours revealed nonuniform curvature in both collagen types, which persisted after surface drying and molecular dehydration, owing to robust collagen–mica adsorption. In addition, the angle between tangent vectors at the ends of molecular segments followed a non-Gaussian probability distribution, indicative of nonequilibrium quenching of fluctuations upon adsorption to mica. These results suggest that collagen either possesses an intrinsic three-dimensional curvature in solution or acquires a two-dimensional curvature upon adsorption. The first scenario has implications for the self-assembly and elasticity of collagen fibrils, whereas the second has implications in biomaterial design and tissue-engineering strategies.</div></div><div><div><span><figure><span><img><ol><li><span><span>Download: <span>Download high-res image (173KB)</span></span></span></li><li><span><span>Download: <span>Download full-size image</span></span></span></li></ol></span></figure></span></div></div>","PeriodicalId":30,"journal":{"name":"Biomacromolecules","volume":"27 8","pages":"Pages 5538-5545"},"PeriodicalIF":5.9,"publicationDate":"2026-08-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148693781","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Ligno-Suberized Fruit Periderm as a Mechanically Reinforced Biomacromolecular Composite","authors":"Yaarit Kutsher,&nbsp;Ekram Wassel,&nbsp;Austin Laviano,&nbsp;Jorge Carvajal,&nbsp;Ekaterina Manasherova,&nbsp;Viktoria V. Zeisler-Diehl,&nbsp;Lukas Schreiber,&nbsp;Ruth E. Stark,&nbsp;Hagai Cohen","doi":"10.1021/acs.biomac.6c00879","DOIUrl":"10.1021/acs.biomac.6c00879","url":null,"abstract":"<div><div>Plant surfaces are biomacromolecular composites whose organization determines barrier performance. We examined the transition from a cutin-dominated cuticle in common cucumber to a ligno-suberized periderm in Sikkim cucumber. Multiscale microscopy and histochemistry resolved a developmental shift from a smooth epidermis to a multilayered phellem characterized by distinct suberin lamellae and lignin deposition. GC-MS-based profiling revealed that periderm formation involves a shift from C16/C18 cutin monomers to an enrichment in &gt;C20 very-long-chain aliphatics (fatty acids, alcohols, hydroxy acids) and phenolics like ferulic acid, hydroxybenzoic acids, and <em>p</em>-hydroxyphenyl, guaiacyl, and syringyl lignin moieties. ssNMR confirmed the increase in oxygenated and phenolic-rich polymer assemblies, consistent with higher cross-link density. Accordingly, peridermal surfaces exhibited significantly enhanced stiffness, adhesion, and elastic resistance. DSC revealed significant elevations in glass transition temperatures (<em>T</em> _g) from 11 °C to 60 °C. These findings establish the fruit periderm as a mechanically robust, thermally stable composite model for sustainable biopolymer design.</div></div><div><div><span><figure><span><img><ol><li><span><span>Download: <span>Download high-res image (87KB)</span></span></span></li><li><span><span>Download: <span>Download full-size image</span></span></span></li></ol></span></figure></span></div></div>","PeriodicalId":30,"journal":{"name":"Biomacromolecules","volume":"27 8","pages":"Pages 5570-5580"},"PeriodicalIF":5.9,"publicationDate":"2026-08-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148389408","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Poly(furfuryl alcohol) as a Surface Modifier for Cellulose Nanocrystals Reinforced HDPE Nanocomposites","authors":"Marlon Bender Bueno Rodrigues,&nbsp;Mariane Weirich Bosenbecker,&nbsp;Amanda Dantas de Oliveira,&nbsp;Silvana I. Wolke,&nbsp;Willian Cézar Nadaleti,&nbsp;Neftali Lenin Villarreal Carreno,&nbsp;Rafael de Avila Delucis,&nbsp;André Luiz Missio","doi":"10.1021/acs.biomac.6c00329","DOIUrl":"10.1021/acs.biomac.6c00329","url":null,"abstract":"<div><div>To overcome the thermodynamic incompatibility between hydrophilic cellulose nanocrystals (CNCs) and nonpolar polyolefins without relying on traditional fossil-based or solvent-heavy covalent compatibilizers, this study introduces a fully biobased, noncovalent strategy. We propose the <em>in situ</em> aqueous polymerization of poly­(furfuryl alcohol) (PFA) to create a hydrophobic core–shell morphology around CNCs, enabling efficient melt-blending with high-density polyethylene (HDPE). Morphological and spectroscopic analyses confirmed the successful physical encapsulation, preserving the nanocrystals’ structural integrity. Consequently, the PFA-modified nanocomposites exhibited robust interfacial adhesion, achieving a 42% increase in Young’s modulus (1856 MPa) alongside enhanced specific strength. Furthermore, the PFA shell acted as an effective thermal barrier, increasing the CNC degradation onset from 250 to 360 °C, and enhanced matrix crystallinity by 9.7%. This facile, green modification distinguishes itself by bridging the polarity gap without toxic solvents, offering a highly scalable route for sustainable structural biocomposites.</div></div><div><div><span><figure><span><img><ol><li><span><span>Download: <span>Download high-res image (273KB)</span></span></span></li><li><span><span>Download: <span>Download full-size image</span></span></span></li></ol></span></figure></span></div></div>","PeriodicalId":30,"journal":{"name":"Biomacromolecules","volume":"27 8","pages":"Pages 5164-5178"},"PeriodicalIF":5.9,"publicationDate":"2026-08-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148395463","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Understanding Processing–Structure–Property Relationships in Spun Spidroin-Mimetic Fibers Using Molecular Dynamics Simulation","authors":"Jeongae Kim,&nbsp;R. Helen Zha,&nbsp;Yunfeng Shi","doi":"10.1021/acs.biomac.6c00520","DOIUrl":"10.1021/acs.biomac.6c00520","url":null,"abstract":"<div><div>Considering the tensile and elongational forces involved in natural silk spinning, silk fiber production resembles drawing processes in conventional fiber manufacturing. Understanding how protein sequence and “drawing” conditions govern molecular structure and mechanical properties is essential for the rational design of silk materials. Here, we employ a coarse-grained molecular dynamics model to simulate the self-assembly of spidroin-mimetic chains with varying β-sheet-forming (hard) segment contents under different spinning strains and times. The simulations reveal distinct degrees of macromolecular alignment and β-sheet nanocrystal formation. Uniaxial tensile simulations show that spinning strain, rather than time, predominantly dictates mechanical performance through its impact on nanoscale structure. The results show that spidroin-like macromolecules with low hard segment content are the best candidates for achieving simultaneous strengthening and toughening through increased spinning strain. These findings establish design guidelines for optimizing silk performance through the coordinated control of sequence architecture and spinning conditions.</div></div><div><div><span><figure><span><img><ol><li><span><span>Download: <span>Download high-res image (139KB)</span></span></span></li><li><span><span>Download: <span>Download full-size image</span></span></span></li></ol></span></figure></span></div></div>","PeriodicalId":30,"journal":{"name":"Biomacromolecules","volume":"27 8","pages":"Pages 5330-5341"},"PeriodicalIF":5.9,"publicationDate":"2026-08-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148402958","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"An Insect Chitosan/Konjac Glucomannan Multifunctional Photo-Cross-Linking Hydrogel Loaded with a Baicalin Nanodelivery System for Promoting MRSA-Infected Diabetic Wound Healing","authors":"Yingxi Li,&nbsp;Xiao Zhou,&nbsp;Ying Wang,&nbsp;Shuang Liu,&nbsp;Huacheng Tang,&nbsp;Yun Duan,&nbsp;Qing Li,&nbsp;Xuebo Li,&nbsp;Fuchen Jiang,&nbsp;Ang Li,&nbsp;Xiaomin Lai,&nbsp;Qiangnu Zhang,&nbsp;Jun Lu,&nbsp;Meng Gong,&nbsp;Xiaoli Pan","doi":"10.1021/acs.biomac.6c00237","DOIUrl":"10.1021/acs.biomac.6c00237","url":null,"abstract":"<div><div>Traditional wound dressings such as gauze and bandages cannot adequately handle the complex biological features of diabetic wounds, including increased bacterial infection risk and persistent inflammation. Therefore, creating multifunctional wound dressings with diverse biological activities is an essential clinical strategy. This study developed a dual-cross-linked photopolymerizable hydrogel (Q/O/Z@B/UV) for treating MRSA-infected diabetic wounds. The hydrogel integrates a network of quaternized insect chitosan and methacrylate-oxidized konjac glucomannan with a baicalin-modified zeolitic imidazolate framework-8 nanosystem. The resulting hydrogels exhibit excellent mechanical properties, biocompatibility, degradability, hemostatic effects, and antimicrobial activity. The Z@B system further enhances antibacterial, antioxidant, and anti-inflammatory activities and also promotes cell proliferation and differentiation. In a full-thickness skin defect model using MRSA-infected diabetic rats, Q/O/Z@B/UV significantly accelerated wound closure, promoted collagen deposition, suppressed inflammatory factor expression, and enhanced angiogenesis. Overall, this multifunctional hydrogel shows great potential for treating MRSA-infected diabetic wounds.</div></div><div><div><span><figure><span><img><ol><li><span><span>Download: <span>Download high-res image (123KB)</span></span></span></li><li><span><span>Download: <span>Download full-size image</span></span></span></li></ol></span></figure></span></div></div>","PeriodicalId":30,"journal":{"name":"Biomacromolecules","volume":"27 8","pages":"Pages 5115-5138"},"PeriodicalIF":5.9,"publicationDate":"2026-08-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148434350","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}