A branching point thermo and pH dual-responsive hyperbranched polymer based on poly(N-vinylcaprolactam) and poly(N,N-diethyl aminoethyl methacrylate)

2013 ◽  
Vol 4 (9) ◽  
pp. 2850 ◽  
Author(s):  
Wei Tian ◽  
Xiao-ying Wei ◽  
Yu-yang Liu ◽  
Xiao-dong Fan
Keyword(s):  
Hyperbranched Polymer ◽  
Dual Responsive ◽  
Branching Point

Design of dual-responsive nanocarries with high drug loading capacity based on hollow mesoporous organosilica nanoparticles

2019 ◽  
Vol 233 ◽  
pp. 230-235 ◽  
Author(s):  
Li-li Lu ◽  
Wen-ya Xiong ◽  
Jun-bin Ma ◽  
Tian-fang Gao ◽  
Si-yuan Peng ◽  
...  
Keyword(s):  
Drug Loading ◽  
Loading Capacity ◽  
High Drug ◽  
Dual Responsive ◽  
Mesoporous Organosilica ◽  
High Drug Loading

O-nitrobenzyl Liposomes with Dual-responsive Release Capabilities for Drug Delivery

2021 ◽  
pp. 116016
Author(s):  
Weihe Yao ◽  
Chenyu Liu ◽  
Ning Wang ◽  
Hengjun Zhou ◽  
Farishta Shafiq ◽  
...  
Keyword(s):  
Drug Delivery ◽  
Dual Responsive

Core/Shell Dual‐Responsive Nanocarriers via Iron‐Mineralized Electrostatic Self‐Assembly for Precise Pesticide Delivery

2021 ◽  
pp. 2102027
Author(s):  
Da‐xia Zhang ◽  
Jiang Du ◽  
Rui Wang ◽  
Jian Luo ◽  
Tong‐fang Jing ◽  
...  
Keyword(s):  
Self Assembly ◽  
Core Shell ◽  
Dual Responsive

Nitrone Mediated Coupling of Hyperbranched Polymer Radicals

2017 ◽  
Vol 218 (15) ◽  
pp. 1700069 ◽  
Author(s):  
Min Du ◽  
Chang Deng ◽  
Xiaoran Wu ◽  
Huarong Liu ◽  
Hewen Liu
Keyword(s):  
Hyperbranched Polymer

scholarly journals Modeled 3D-Structures of Proteobacterial Transglycosylases from Glycoside Hydrolase Family 17 Give Insight in Ligand Interactions Explaining Differences in Transglycosylation Products

2021 ◽  
Vol 11 (9) ◽  
pp. 4048
Author(s):  
Javier A. Linares-Pastén ◽  
Lilja Björk Jonsdottir ◽  
Gudmundur O. Hreggvidsson ◽  
Olafur H. Fridjonsson ◽  
Hildegard Watzlawick ◽  
...  
Keyword(s):  
Glycoside Hydrolase ◽  
Ligand Docking ◽  
Glycoside Hydrolase Family ◽  
Ligand Interactions ◽  
Tim Barrel ◽  
Branching Point ◽  
The Difference ◽  
Dynamics Simulations ◽  
And Function ◽  
Hydrolase Family

The structures of glycoside hydrolase family 17 (GH17) catalytic modules from modular proteins in the ndvB loci in Pseudomonas aeruginosa (Glt1), P. putida (Glt3) and Bradyrhizobium diazoefficiens (previously B. japonicum) (Glt20) were modeled to shed light on reported differences between these homologous transglycosylases concerning substrate size, preferred cleavage site (from reducing end (Glt20: DP2 product) or non-reducing end (Glt1, Glt3: DP4 products)), branching (Glt20) and linkage formed (1,3-linkage in Glt1, Glt3 and 1,6-linkage in Glt20). Hybrid models were built and stability of the resulting TIM-barrel structures was supported by molecular dynamics simulations. Catalytic amino acids were identified by superimposition of GH17 structures, and function was verified by mutagenesis using Glt20 as template (i.e., E120 and E209). Ligand docking revealed six putative subsites (−4, −3, −2, −1, +1 and +2), and the conserved interacting residues suggest substrate binding in the same orientation in all three transglycosylases, despite release of the donor oligosaccharide product from either the reducing (Glt20) or non-reducing end (Glt1, Gl3). Subsites +1 and +2 are most conserved and the difference in release is likely due to changes in loop structures, leading to loss of hydrogen bonds in Glt20. Substrate docking in Glt20 indicate that presence of covalently bound donor in glycone subsites −4 to −1 creates space to accommodate acceptor oligosaccharide in alternative subsites in the catalytic cleft, promoting a branching point and formation of a 1,6-linkage. The minimum donor size of DP5, can be explained assuming preferred binding of DP4 substrates in subsite −4 to −1, preventing catalysis.

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