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1. TurboID ‐based proteomic profiling reveals proxitome of ASK1 and CUL1 of the SCF ubiquitin ligase in plants

   https://doi.org/10.1111/nph.20014  

   Sun, Fuai; Hamada, Natalie; Montes, Christian; Li, Yuanyuan; Meier, Nathan_D; Walley, Justin_W; Dinesh‐Kumar, Savithramma_P; Shabek, Nitzan (July 2024, New Phytologist)
2. 2.2.2-Cryptand complexes of neptunium( iii ) and plutonium( iii )

   https://doi.org/10.1039/D1CC05904A  

   Goodwin, Conrad A.; Ciccone, Sierra R.; Bekoe, Samuel; Majumdar, Sourav; Scott, Brian L.; Ziller, Joseph W.; Gaunt, Andrew J.; Furche, Filipp; Evans, William J. (January 2022, Chemical Communications)

   New coordination environments are reported for Np( iii ) and Pu( iii ) based on pilot studies of U( iii ) in 2.2.2-cryptand (crypt). The U( iii )-in-crypt complex, [U(crypt)I 2 ][I], obtained from the reaction between UI 3 and crypt, is treated with Me 3 SiOTf (OTf = O 3 SCF 3 ) in benzene to form the [U(crypt)(OTf) 2 ][OTf] complex. Similarly, the isomorphous Np( iii ) and Pu( iii ) complexes were obtained similarly starting from [AnI 3 (THF) 4 ]. All three complexes (1-An; An = U, Np, Pu) contain an encapsulated actinide in a THF-soluble complex. Absorption spectroscopy and DFT calculations are consistent with 5f 3 U( iii ), 5f 4 Np( iii ), and 5f 5 Pu( iii ) electron configurations. 

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3. Metal–ligand and hydrogen bonding in the active site of Fe( iii )-, Mn( iii )- and Co( iii )-myoglobins

   https://doi.org/10.1039/D4DT03246B  

   Freindorf, Marek; Kraka, Elfi (March 2025, Dalton Transactions)

   We investigated in this work strength of metal–ligand and hydrogen bonding in complexes formed between Fe, Mn, and Co myoglobin and molecular ligands such as methanol, water, nitrite, and azide involving ε and δ protonation forms of distal histidine. 

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4. Substrates (Acyl‐ CoA and Diacylglycerol) Entry and Products ( CoA and Triacylglycerol) Egress Pathways in DGAT1

   https://doi.org/10.1002/jcc.70108  

   Lee, Hwayoung; Im, Wonpil (April 2025, Journal of Computational Chemistry)

   ABSTRACT Diacylglycerol O‐acyltransferase 1 (DGAT1) is an integral membrane protein that uses acyl‐coenzyme A (acyl‐CoA) and diacylglycerol (DAG) to catalyze the formation of triacylglycerides (TAGs). The acyl transfer reaction occurs between the activated carboxylate group of the fatty acid and the free hydroxyl group on the glycerol backbone of DAG. However, how the two substrates enter DGAT1's catalytic reaction chamber and interact with DGAT1 remains elusive. This study aims to explore the structural basis of DGAT1's substrate recognition by investigating each substrate's pathway to the reaction chamber. Using a human DGAT1 cryo‐EM structure in complex with an oleoyl‐CoA substrate, we designed two different all‐atom molecular dynamics (MD) simulation systems: DGAT1^away(both acyl‐CoA and DAG away from the reaction chamber) and DGAT1^bound(acyl‐CoA bound in and DAG away from the reaction chamber). Our DGAT1^awaysimulations reveal that acyl‐CoA approaches the reaction chamber via interactions with positively charged residues in transmembrane helix 7. DGAT1^boundsimulations show DAGs entering into the reaction chamber from the cytosol leaflet. The bound acyl‐CoA's fatty acid lines up with the headgroup of DAG, which appears to be competent to TAG formation. We then converted them into TAG and coenzyme (CoA) and used adaptive biasing force (ABF) simulations to explore the egress pathways of the products. We identify their escape routes, which are aligned with their respective entry pathways. Visualization of the substrate and product pathways and their interactions with DGAT1 is expected to guide future experimental design to better understand DGAT1 structure and function. 

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5. Development of a Bioinspired, Self‐Adhering, and Drug‐Eluting Laryngotracheal Patch

   https://doi.org/10.1002/lary.29182  

   Miar, Solaleh; Dion, Gregory R.; Montelongo, Sergio; Ong, Joo L.; Bizios, Rena; Guda, Teja (October 2020, The Laryngoscope)

   null (Ed.)

   Objectives/Hypothesis Novel laryngotracheal wound coverage devices are limited by complex anatomy, smooth surfaces, and dynamic pressure changes and airflow during breathing. We hypothesize that a bioinspired mucoadhesive patch mimicking how geckos climb smooth surfaces will permit sutureless wound coverage and also allow drug delivery. Study Design ex‐vivo. Methods Polycaprolactone (PCL) fibers were electrospun onto a substrate and polyethylene glycol (PEG) – acrylate flocks in varying densities were deposited to create a composite patch. Sample topography was assessed with laser profilometry, material stiffness with biaxial mechanical testing, and mucoadhesive testing determined cohesive material failure on porcine tracheal tissue. Degradation rate was measured over 21 days in vitro along with dexamethasone drug release profiles. Material handleability was evaluated via suture retention and in cadaveric larynges. Results Increased flocking density was inversely related to cohesive failure in mucoadhesive testing, with a flocking density of PCL‐PEG‐2XFLK increasing failure strength to 6880 ± 1810 Pa compared to 3028 ± 791 in PCL‐PEG‐4XFLK density and 1182 ± 262 in PCL‐PEG‐6XFLK density. The PCL‐PEG‐2XFLK specimens had a higher failure strength than PCL alone (1404 ± 545 Pa) or PCL‐PEG (2732 ± 840). Flocking progressively reduced composite stiffness from 1347 ± 15 to 763 ± 21 N/m. Degradation increased from 12% at 7 days to 16% after 10 days and 20% after 21 days. Cumulative dexamethasone release at 0.4 mg/cm2 concentration was maintained over 21 days. Optimized PCL‐PEG‐2XFLK density flocked patches were easy to maneuver endoscopically in laryngeal evaluation. Conclusions This novel, sutureless, patch is a mucoadhesive platform suitable to laryngeal and tracheal anatomy with drug delivery capability. 

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