2篇
您的检索式：作者名="Runsha Chen"
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| 1 | An ESIPT-based NIR-fluorescent probe for exosome labeling and in situ imaging显示文摘Exosomes play significant roles in physiological and tumorigenic processes and it is desirable to visualize and track the exosomes.Herein,a novel amphiphilic fluorescent probe HBT-Exo based on excited-state intramolecular proton transfer(ESIPT)mechanism is reported for exosome-labeling.Its ESIPT characteristics were confirmed by both theory calculation and experimental observation,which enable the probe to show a large Stokes shift as well as near-infrared(NIR)keto-form emission.HBT-Exo displayed excellent biocompatibility and remarkable efficiency for exosome-labeling in gastric cancer cells.Furthermore,the labeled exosomes were successfully applied for the real-time in situ imaging in mouse models. | Jipeng Ding Runsha Xiao Anyao Bi Guanyang Chen Nengwei Zhang Zihua Chen Xueping Feng Wenbin Zeng | 2023 | Chinese Chemical Letters2023，34，11： | 0 |
| 2 | Crystal structure of the GDSL family esterase EstL5 in complex with PMSF reveals a branch channel of the active site pocket显示文摘Esterases/lipases from the GDSL family have potential applications in the hydrolysis and synthesis of important esters of pharmaceutical,food,and biotechnical interests.However,the structural and functional understanding of GDSL enzymes is still limited.Here,we report the crystal structure of the GDSL family esterase EstL5 complexed with PMSF at 2.34Åresolution.Intriguingly,the PMSF binding site is not located at the active site pocket but is situated in a surface cavity.At the active site,we note that there is a trapped crystallization solvent 1,6-hexanediol,which mimics the bound ester chain,allowing for further definition of the active site pocket of EstL5.The most striking structural feature of EstL5 is the presence of a unique channel,which extends approximately 18.9Å,with a bottleneck radius of 6.8Å,connecting the active-site pocket and the surface cavity.Replacement of Ser205 with the bulk aromatic residue Trp or Phe could partially block the channel at one end and perturb its access.Reduced enzymatic activity is found in the EstL5 S205W and EstL5 S205F mutants,suggesting the functional relevance of the channel to enzyme catalysis.Our study provides valuable information regarding the properties of the GDSL-family enzymes for designing more efficient and robust biocatalysts. | Runsha Chen Xuechun Gao Ting Nie Jinhong Wu Lin Wang Ali Osman Yan Feng Xianghong Li Yong Zhang | 2023 | Acta Biochimica et Biophysica Sinica2023，55，11： | 0 |
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