Exploiting the Benefits of Homogeneous and Heterogeneous Biocatalysis: Tuning the Molecular Interaction of Enzymes with Solvents via Polymer Modification

ACS Catalysis ◽  
2018 ◽  
Vol 8 (12) ◽  
pp. 11579-11588 ◽  
Author(s):  
Garrett R. Chado ◽  
Elijah N. Holland ◽  
Andrew K. Tice ◽  
Mark P. Stoykovich ◽  
Joel L. Kaar
Keyword(s):  
Molecular Interaction ◽  
Polymer Modification ◽  
Heterogeneous Biocatalysis

Functional Poly(p-Xylylene)s via Chemical Reduction of Poly(p-Phenylene Vinylene)s

2019 ◽  
Author(s):  
Ain Uddin ◽  
Weifan Sang ◽  
Yong Gao ◽  
Kyle Plunkett
Keyword(s):  
Film Formation ◽  
Chemical Reduction ◽  
Water Soluble ◽  
Phenylene Vinylene ◽  
Polymer Modification ◽  
Polymer Backbone ◽  
Crosslinking Process ◽  
Conducting Membranes ◽  
In Situ Crosslinking

The synthesis of poly(p-xylylene)s (PPXs) with sidechains containing alkyl bromide functionality, and their post-polymer modification, is described. The PPXs were prepared by a diimide hydrogenation of poly(p-phenylene vinylene)s (PPVs) that were originally synthesized by a Gilch polymerization. The polymer backbone reduction was carried out with hydrazine hydrate in toluene at 80 °C to provide polymers with the sidechain-containing bromide functionality intact. To demonstrate post-polymer modification of the sidechains, the resulting PPX polymers were modified with trimethylamine to form tetraalkylammonium ion functionality and were evaluated as anion conducting membranes. While PPX homopolymers containing tetralkylammonium ions were completely water soluble and not able to form valuable films, PPX copolymers containing mixed tetraalkylammonium ions and hydrophobic chains were capable of film formation and alkaline stability. In addition, an in situ crosslinking process that used N,N,N',N'-tetramethyl-1,6-hexanediamine during the tetraalkylammonium formation of brominated PPX polymers was also evaluated and gave reasonable films with conductivities of ~10 mS-cm-1.

Functional Poly(p-Xylylene)s via Chemical Reduction of Poly(p-Phenylene Vinylene)s

2019 ◽  
Author(s):  
Ain Uddin ◽  
Weifan Sang ◽  
Yong Gao ◽  
Kyle Plunkett
Keyword(s):  
Film Formation ◽  
Chemical Reduction ◽  
Water Soluble ◽  
Phenylene Vinylene ◽  
Polymer Modification ◽  
Polymer Backbone ◽  
Crosslinking Process ◽  
Conducting Membranes ◽  
In Situ Crosslinking

The synthesis of poly(p-xylylene)s (PPXs) with sidechains containing alkyl bromide functionality, and their post-polymer modification, is described. The PPXs were prepared by a diimide hydrogenation of poly(p-phenylene vinylene)s (PPVs) that were originally synthesized by a Gilch polymerization. The polymer backbone reduction was carried out with hydrazine hydrate in toluene at 80 °C to provide polymers with the sidechain-containing bromide functionality intact. To demonstrate post-polymer modification of the sidechains, the resulting PPX polymers were modified with trimethylamine to form tetraalkylammonium ion functionality and were evaluated as anion conducting membranes. While PPX homopolymers containing tetralkylammonium ions were completely water soluble and not able to form valuable films, PPX copolymers containing mixed tetraalkylammonium ions and hydrophobic chains were capable of film formation and alkaline stability. In addition, an in situ crosslinking process that used N,N,N',N'-tetramethyl-1,6-hexanediamine during the tetraalkylammonium formation of brominated PPX polymers was also evaluated and gave reasonable films with conductivities of ~10 mS-cm-1.

MOLECULAR INTERACTION THROUGH FREE VOLUME AND INTERNAL PRESSURE OF AQUEOUS AMINO ACIDS AT 308.15 K

2014 ◽  
Author(s):  
Amardeep Shende Hemant Baradkar Vilas Tabhane Amardeep Shende Hemant Baradkar Vilas Tabhane ◽  
Keyword(s):  
Amino Acids ◽  
Internal Pressure ◽  
Free Volume ◽  
Molecular Interaction

In silico Screening and Molecular Interaction Studies of Tetrahydrocannabinol and its Derivatives with Acetylcholine Binding Protein

2018 ◽  
Vol 12 (2) ◽  
pp. 181-190 ◽  
Author(s):  
Priya P. Panigrahi ◽  
Ramit Singla ◽  
Ankush Bansal ◽  
Moacyr Comar Junior ◽  
Vikas Jaitak ◽  
...  
Keyword(s):  
Molecular Interaction ◽  
In Silico ◽  
Binding Protein ◽  
In Silico Screening ◽  
Acetylcholine Binding Protein ◽  
Interaction Studies

Mixed matrix membranes with molecular-interaction-driven tunable free volumes for efficient bio-fuel recovery

2015 ◽  
Vol 3 (8) ◽  
pp. 4510-4521 ◽  
Author(s):  
Gongping Liu ◽  
Wei-Song Hung ◽  
Jie Shen ◽  
Qianqian Li ◽  
Yun-Hsuan Huang ◽  
...  
Keyword(s):  
Polymer Chain ◽  
Molecular Interactions ◽  
Molecular Interaction ◽  
Chain Conformation ◽  
Mixed Matrix Membranes ◽  
Mixed Matrix ◽  
Polymer Chain Conformation ◽  
Matrix Membranes

Molecular interactions were constructed to control polymer chain conformation to fabricate mixed matrix membranes with tunable free volumes, exhibiting simultaneously improved butanol permeability and selectivity.

scholarly journals A Region of the Myosin Rod Important for Interaction With Paramyosin in Caenorhabditis elegans Striated Muscle

Genetics ◽  
2000 ◽  
Vol 156 (2) ◽  
pp. 631-643
Author(s):  
Pamela E Hoppe ◽  
Robert H Waterston
Keyword(s):  
Caenorhabditis Elegans ◽  
Heavy Chain ◽  
Molecular Interaction ◽  
Striated Muscle ◽  
Genetic Interaction ◽  
Specific Interaction ◽  
Thick Filament ◽  
Parallel Arrangement ◽  
Myosin Rod

Abstract The precise arrangement of molecules within the thick filament, as well as the mechanisms by which this arrangement is specified, remains unclear. In this article, we have exploited a unique genetic interaction between one isoform of myosin heavy chain (MHC) and paramyosin in Caenorhabditis elegans to probe the molecular interaction between MHC and paramyosin in vivo. Using chimeric myosin constructs, we have defined a 322-residue region of the MHC A rod critical for suppression of the structural and motility defects associated with the unc-15(e73) allele. Chimeric constructs lacking this region of MHC A either fail to suppress, or act as dominant enhancers of, the e73 phenotype. Although the 322-residue region is required for suppression activity, our data suggest that sequences along the length of the rod also play a role in the isoform-specific interaction between MHC A and paramyosin. Our genetic and cell biological analyses of construct behavior suggest that the 322-residue region of MHC A is important for thick filament stability. We present a model in which this region mediates an avid interaction between MHC A and paramyosin in parallel arrangement in formation of the filament arms.

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