02609nas a2200325   4500008004100000022001400041245011700055210006900172260000800241300001400249490000600263520156100269653002701830653001201857653002201869653001501891653001801906100002301924700001601947700001701963700002301980700001802003700001902021700001602040700002202056700002502078700002502103700002402128856013102152       2022                        eng d  a2637-610500aAlgal biomass-loaded hydrogel scaffolds as a biomimetic platform with antibacterial and wound healing activities0 aAlgal biomassloaded hydrogel scaffolds as a biomimetic platform   cAUG  a5800-58120 v43 a<p>
	The confluence of hydrogel scaffolds and dried algal biomass (AB), consisting of all the bioactive compounds, offers the possibility to facilitate wound healing while simultaneously instilling antibacterial benefits. For this purpose, a single-step synthesis of algal (Chlorella sorokiniana) biomass-loaded hydrogel scaffolds (AHS) was achieved. C. sorokiniana has been used in different areas for several years and has proved attractive to the pharmaceutical and cosmetic industries. Of note, the presence of phytochemicals and various bioactive compounds provides an added health benefit. Hitherto, we report AHS with accelerated wound healing along with potent anti-inflammatory and antibacterial properties. AHS consisting of different concentrations of AB was applied for 14 days on excisional wounds in mice. Microscopic analyses, assessment of proinflammatory and anti-inflammatory cytokines, and histological studies were performed to investigate wound healing. These scaffolds were extensively characterized and studied using Fourier transform infrared, X-ray diffraction, Raman, atomic force microscopy, transmission electron microscopy, scanning electron microscopy, swelling, rheological, thermal, and mechanical analyses. AHS have excellent biocompatibility in addition to significant antibacterial activity against Escherichia coli (99%) and Staphylococcus aureus (98%). We believe that the as-synthesized AHS have the potential to broaden the arsenal of more effective wound healing processes along with antibacterial activities.</p>
10aantibacterial activity10aBiomass10ahydrogel scaffold10amicroalgae10awound Healing1 aAgarwal, Aakanksha1 aKumar, Arun1 aGarg, Piyush1 aChakraborty, Arnab1 aVerma, Ranjan1 aSarwat, Maryam1 aGupta, Ajay1 aSasmal, Pijus, K.1 aVerma, Yogesh, Kumar1 aChowdhury, Chiranjit1 aMukherjee, Monalisa  uhttps://library.ncl.res.in/content/algal-biomass-loaded-hydrogel-scaffolds-biomimetic-platform-antibacterial-and-wound-healing02635nas a2200265   4500008004100000022001400041245012400055210006900179260000900248300001400257490000700271520171400278100002401992700002302016700002002039700002602059700002102085700002302106700002102129700002602150700002402176700002202200700002402222856012302246       2025                        eng d  a1554-892900aEnzymatic pathway for kupyaphore degradation in mycobacterium tuberculosis: mechanism of metal homeostasis and turnover0 aEnzymatic pathway for kupyaphore degradation in mycobacterium tu  cJUN   a1492-15040 v203 a<p>
	Metallophores are essential for metal homeostasis, regulating availability, and mediating host-pathogen interactions. Kupyaphores are specialized metallophores produced by Mycobacterium tuberculosis (Mtb) that primarily chelate zinc to support bacterial survival. Elevated kupyaphore levels early in infection highlight their importance, while their rapid decline, despite increasing bacterial loads, indicates tightly regulated mechanisms of production, consumption, and degradation. However, the processes driving kupyaphore catabolism and their role in preventing zinc toxicity in Mtb remain unclear. Here, we show that covalent modification of the isonitrile moiety in kupyaphores releases zinc, triggering degradation through a sequential three-step enzymatic pathway encoded by Mtb. Isonitrile hydratase converts isonitrile groups into formamides, which are subsequently processed into amines by N-substituted formamide deformylase and ultimately oxidized to beta-ketoesters by amine oxidases. The biological significance of this pathway is underscored by the upregulation of these genes under metal-depleted and biofilm-forming conditions. Mutant Mtb strains lacking these genes exhibit impaired growth in metal-limiting environments and reduced levels of biofilm formation. Catalytic intermediates detected in Mtb cultures and infected mouse lung tissues confirm the pathway's in vivo activity. Further, genome mining reveals that similar enzymes are conserved across organisms producing isonitrile-containing metabolites, emphasizing the broader importance of this pathway. Understanding these processes could pave the way for novel therapeutic strategies targeting kupyaphore catabolism.</p>
1 aBhosale, Rashmi, S.1 aChakraborty, Arnab1 aWong, Tsung-Yun1 aMasal, Dattatraya, P.1 aChoudhury, Rahul1 aSrivastava, Sonali1 aReddy, Srinivasa1 aAldrich, Courtney, C.1 aKamat, Siddhesh, S.1 aMohanty, Debasisa1 aGokhale, Rajesh, S.  uhttps://library.ncl.res.in/content/enzymatic-pathway-kupyaphore-degradation-mycobacterium-tuberculosis-mechanism-metal