scholarly journals Rational Design of Bioinspired Nanocomposites with Tunable Catalytic Activity

Author(s):  
Hans C. Hendrikse ◽  
Alejo Aguirre ◽  
Arno van der Weijden ◽  
Anne S. Meeussen ◽  
Fernanda Neira D’Angelo ◽  
...  
2019 ◽  
Vol 126 ◽  
pp. 229-237 ◽  
Author(s):  
Naeem Mahmood Ashraf ◽  
Akshaya Krishnagopal ◽  
Aadil Hussain ◽  
David Kastner ◽  
Ahmed Mahmoud Mohammed Sayed ◽  
...  

2018 ◽  
Vol 1 (3) ◽  
pp. 1150-1163 ◽  
Author(s):  
Wei Cai ◽  
Qin Zhong ◽  
Dongyu Wang ◽  
Yunxia Zhao ◽  
Mindong Chen ◽  
...  

2016 ◽  
Vol 6 (13) ◽  
pp. 5102-5115 ◽  
Author(s):  
Biplab Banerjee ◽  
Ramana Singuru ◽  
Sudipta K. Kundu ◽  
Karnekanti Dhanalaxmi ◽  
Linyi Bai ◽  
...  

Core–shell catalytic nanoreactor was designed, exhibiting high catalytic activity for levulinic acid hydrogenation.


Synthesis ◽  
2018 ◽  
Vol 50 (07) ◽  
pp. 1499-1510 ◽  
Author(s):  
Wei Chen ◽  
Xiao-Yan Lu ◽  
Bei-Hua Xu ◽  
Wei-guo Yu ◽  
Zi-niu Zhou ◽  
...  

Eight precatalysts containing carboxylic-functionalized thiourea ligands are prepared and their activities and recyclability are evaluated in aerobic aqueous Suzuki–Miyaura reactions. A bulky monothiourea–Pd complex, functionalized with four carboxylic groups, shows the best activity and recyclability in the coupling of aryl bromides with arylboronic acids. The catalyst can be reused at least five times without any significant reduction in its catalytic activity. TEM analysis and the confirmed catalytic activity of the observed black precipitate reveal that Pd nanoparticles are formed during the reactions and are stabilized by the carboxylic-functionalized thiourea ligands.


Author(s):  
Christos S. Karamitros ◽  
Catrina M. Somody ◽  
Giulia Agnello ◽  
Scott Rowlinson

Human thymidine phosphorylase (HsTP) is an enzyme with important implications in the field of rare metabolic diseases. Defective mutations of HsTP lead to mitochondrial neurogastrointestinal encephalomyopathy (MNGIE), a disease with a high unmet medical need that is associated with severe neurological and gastrointestinal complications. Current efforts focus on the development of an enzyme replacement therapy (ERT) using the Escherichia coli ortholog (EcTP). However, bacterial enzymes are counter-indicated for human therapeutic applications because they are recognized as foreign by the human immune system, thereby eliciting adverse immune responses and raising significant safety and efficacy risks. Thus, it is critical to utilize the HsTP enzyme as starting scaffold for pre-clinical drug development, thus de-risking the safety concerns associated with the use of bacterial enzymes. However, HsTP expresses very poorly in E. coli, whereas its PEGylation, a crucial chemical modification for achieving long serum persistence of therapeutic enzymes, is highly inefficient and negatively affects its catalytic activity. Here we focused on the engineering of the recombinant expression profile of HsTP in E. coli cells, as well as on the optimization of its PEGylation efficiency aiming at the development of an alternative therapeutic approach for MNGIE. We show that phylogenetic and structural analysis of proteins can provide important insights for the rational design of N’-terminus-truncation constructs which exhibit significantly improved recombinant expression levels. In addition, we developed and implemented a criteria-driven rational surface engineering strategy for the substitution of arginine-to-lysine and lysine-to-arginine residues to achieve more efficient, homogeneous and reproducible PEGylation without negatively affecting the enzymatic catalytic activity upon PEGylation. Collectively, our proposed strategies provide an effective way to optimize enzyme PEGylation and E. coli recombinant expression and are likely applicable for other proteins and enzymes.


2019 ◽  
Vol 10 (1) ◽  
Author(s):  
Bin Dong ◽  
Yuchen Pei ◽  
Nourhan Mansour ◽  
Xuemei Lu ◽  
Kai Yang ◽  
...  

Abstract Nanoconfinement could dramatically change molecular transport and reaction kinetics in heterogeneous catalysis. Here we specifically design a core-shell nanocatalyst with aligned linear nanopores for single-molecule studies of the nanoconfinement effects. The quantitative single-molecule measurements reveal unusual lower adsorption strength and higher catalytic activity on the confined metal reaction centres within the nanoporous structure. More surprisingly, the nanoconfinement effects on enhanced catalytic activity are larger for catalysts with longer and narrower nanopores. Experimental evidences, including molecular orientation, activation energy, and intermediate reactive species, have been gathered to provide a molecular level explanation on how the nanoconfinement effects enhance the catalyst activity, which is essential for the rational design of highly-efficient catalysts.


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