Retraction notice to “Adsorption of Crystal violet on raw and acid-treated montmorillonite, K10, in aqueous suspension” [J. Environ. Manag. 171, 2016, 1–10]

Recently, a new sort of nano-composites has been prepared by incorporating such fine particles as metal oxide microcrystallites and organic polymers into the interlayer space of montmorillonite. Owing to their extremely large specific surface area, the nano-composites are finding wide application[1∼3]. However, the topographic features of the microstructures have not been elucidated as yet In the present work, the microstructures of iron oxide-pillared montmorillonite have been investigated by high-resolution transmission electron microscopy.Iron oxide-pillared montmorillonite was prepared through the procedure essentially the same as that reported by Yamanaka et al. Firstly, 0.125 M aqueous solution of trinuclear acetato-hydroxo iron(III) nitrate, [Fe3(OCOCH3)7 OH.2H2O]NO3, was prepared and then the solution was mixed with an aqueous suspension of 1 wt% clay by continuously stirring at 308 K. The final volume ratio of the latter aqueous solution to the former was 0.4. The clay used was sodium montmorillonite (Kunimine Industrial Co.), having a cation exchange capacity of 100 mequiv/100g. The montmorillonite in the mixed suspension was then centrifuged, followed by washing with deionized water. The washed samples were spread on glass plates, air dried, and then annealed at 673 K for 72 ks in air. The resultant film products were approximately 20 μm in thickness and brown in color.

Download Full-text

RETRACTION NOTICE

Research in Pharmacy and Health Sciences ◽

10.32463/rphs.2020.v06i02.04 ◽

2020 ◽

Vol 06 (02) ◽

pp. 130-130

Author(s):

Isha Patel

Keyword(s):

Retraction Notice

Download Full-text

Mineral/microfibrillated cellulose composite materials: High performance products, applications, and product forms

TAPPI Journal ◽

10.32964/tj17.09.507 ◽

2018 ◽

Vol 17 (09) ◽

pp. 507-515 ◽

Cited By ~ 1

Author(s):

David Skuse ◽

Mark Windebank ◽

Tafadzwa Motsi ◽

Guillaume Tellier

Keyword(s):

Composite Materials ◽

High Performance ◽

Aqueous Suspension ◽

Production Capacity ◽

Cost Savings ◽

Cost Effective ◽

New Materials ◽

Wet Strength ◽

Product Forms ◽

Cellulose Composite

When pulp and minerals are co-processed in aqueous suspension, the mineral acts as a grinding aid, facilitating the cost-effective production of fibrils. Furthermore, this processing allows the utilization of robust industrial milling equipment. There are 40000 dry metric tons of mineral/microfbrillated (MFC) cellulose composite production capacity in operation across three continents. These mineral/MFC products have been cleared by the FDA for use as a dry and wet strength agent in coated and uncoated food contact paper and paperboard applications. We have previously reported that use of these mineral/MFC composite materials in fiber-based applications allows generally improved wet and dry mechanical properties with concomitant opportunities for cost savings, property improvements, or grade developments and that the materials can be prepared using a range of fibers and minerals. Here, we: (1) report the development of new products that offer improved performance, (2) compare the performance of these new materials with that of a range of other nanocellulosic material types, (3) illustrate the performance of these new materials in reinforcement (paper and board) and viscosification applications, and (4) discuss product form requirements for different applications.

Download Full-text

Clinical Trial of Ampicillin Trihydrate Aqueous Suspension on Infectious Skin Diseases

Nishi Nihon Hifuka ◽

10.2336/nishinihonhifu.37.432 ◽

1975 ◽

Vol 37 (3) ◽

pp. 432-435 ◽

Cited By ~ 1

Author(s):

Tadahiko MATSUMOTO ◽

Michiyasu ARIYOSHI

Keyword(s):

Clinical Trial ◽

Skin Diseases ◽

Aqueous Suspension ◽

Ampicillin Trihydrate ◽

Infectious Skin Diseases

Download Full-text

Immobilization of ZnO Suspension on Glass Substrate to Remove Filtration During the Removal of Remazol Red R from Aqueous Solution

JOURNAL OF ADVANCES IN CHEMISTRY ◽

10.24297/jac.v12i6.6990 ◽

2016 ◽

Vol 12 (6) ◽

pp. 4127-4133

Author(s):

Nazmul Kayes ◽

Jalil Miah ◽

Md. Obaidullah ◽

Akter Hossain ◽

Mufazzal Hossain

Keyword(s):

Aqueous Solution ◽

Glass Substrate ◽

Uv Light ◽

Aqueous Suspension ◽

Light Irradiation ◽

Zno Films ◽

Light Sources ◽

Zno Film ◽

Semiconductor Oxides ◽

Remazol Red

Photodegradation of textile dyes in the presence of an aqueous suspension of semiconductor oxides has been of growing interest. Although this method of destruction of dyes is efficient, the main obstacle of applying this technique in the industry is the time and cost involving separation of oxides from an aqueous suspension. In this research, an attempted was made to develop ZnO films on a glass substrate by simple immobilization method for the adsorption and photodegradation of a typical dye, Remazol Red R (RRR) from aqueous solution. Adsorption and photodegradation of RRR were performed in the presence of glass supported ZnO film. Photodegradation of the dye was carried out by varying different parameters such as the catalyst dosage, initial concentrations of RRR, and light sources. The percentage of adsorption as well as photodegradation increased with the amount of ZnO, reaches a maximum and then decreased. Maximum degradation has been found under solar light irradiation as compared to UV-light irradiation. Removal efficiency was also found to be influenced by the pre-sonication of ZnO suspension.

Download Full-text

Target-Templated de novo Design of Macrocyclic D-/L-Peptides: Inhibitors of the PD-1/PD-L1 Interaction

10.26434/chemrxiv.11663337.v3 ◽

2020 ◽

Author(s):

Salvador Guardiola ◽

Monica Varese ◽

Xavier Roig ◽

Jesús Garcia ◽

Ernest Giralt

Keyword(s):

Protein Interactions ◽

Cyclic Peptides ◽

General Framework ◽

Large Scale ◽

De Novo ◽

Inhibitory Effect ◽

Original Text ◽

Protein Protein Interactions ◽

Retraction Notice ◽

Pharmaceutical Properties

NOTE: This preprint has been retracted by consensus from all authors. See the retraction notice in place above; the original text can be found under "Version 1", accessible from the version selector above. ------------------------------------------------------------------------ Peptides, together with antibodies, are among the most potent biochemical tools to modulate challenging protein-protein interactions. However, current structure-based methods are largely limited to natural peptides and are not suitable for designing target-specific binders with improved pharmaceutical properties, such as macrocyclic peptides. Here we report a general framework that leverages the computational power of Rosetta for large-scale backbone sampling and energy scoring, followed by side-chain composition, to design heterochiral cyclic peptides that bind to a protein surface of interest. To showcase the applicability of our approach, we identified two peptides (PD-i3 and PD-i6) that target PD-1, a key immune checkpoint, and work as protein ligand decoys. A comprehensive biophysical evaluation confirmed their binding mechanism to PD-1 and their inhibitory effect on the PD-1/PD-L1 interaction. Finally, elucidation of their solution structures by NMR served as validation of our de novo design approach. We anticipate that our results will provide a general framework for designing target-specific drug-like peptides.

Download Full-text

A Target-Based Method for Designing Heterochiral Cyclic Peptide Binders: De Novo Inhibitors of the PD-1/PD-L1 Interaction

10.26434/chemrxiv.11663337.v2 ◽

2020 ◽

Author(s):

Salvador Guardiola ◽

Monica Varese ◽

Xavier Roig ◽

Jesús Garcia ◽

Ernest Giralt

Keyword(s):

Protein Interactions ◽

Cyclic Peptides ◽

General Framework ◽

Large Scale ◽

Cyclic Peptide ◽

De Novo ◽

Inhibitory Effect ◽

Original Text ◽

Retraction Notice ◽

Pharmaceutical Properties

NOTE: This preprint has been retracted by consensus from all authors. See the retraction notice in place above; the original text can be found under "Version 1", accessible from the version selector above. ------------------------------------------------------------------------ Peptides, together with antibodies, are among the most potent biochemical tools to modulate challenging protein-protein interactions. However, current structure-based methods are largely limited to natural peptides and are not suitable for designing target-specific binders with improved pharmaceutical properties, such as macrocyclic peptides. Here we report a general framework that leverages the computational power of Rosetta for large-scale backbone sampling and energy scoring, followed by side-chain composition, to design heterochiral cyclic peptides that bind to a protein surface of interest. To showcase the applicability of our approach, we identified two peptides (PD-i3 and PD-i6) that target PD-1, a key immune checkpoint, and work as protein ligand decoys. A comprehensive biophysical evaluation confirmed their binding mechanism to PD-1 and their inhibitory effect on the PD-1/PD-L1 interaction. Finally, elucidation of their solution structures by NMR served as validation of our de novo design approach. We anticipate that our results will provide a general framework for designing target-specific drug-like peptides.

Download Full-text

Target-Templated de novo Design of Macrocyclic D-/L-Peptides: Inhibitors of the PD-1/PD-L1 Interaction

10.26434/chemrxiv.11663337 ◽

2020 ◽

Author(s):

Salvador Guardiola ◽

Monica Varese ◽

Xavier Roig ◽

Jesús Garcia ◽

Ernest Giralt

Keyword(s):

Protein Interactions ◽

Cyclic Peptides ◽

General Framework ◽

Large Scale ◽

De Novo ◽

Inhibitory Effect ◽

Original Text ◽

Protein Protein Interactions ◽

Retraction Notice ◽

Pharmaceutical Properties

NOTE: This preprint has been retracted by consensus from all authors. See the retraction notice in place above; the original text can be found under "Version 1", accessible from the version selector above. ------------------------------------------------------------------------ Peptides, together with antibodies, are among the most potent biochemical tools to modulate challenging protein-protein interactions. However, current structure-based methods are largely limited to natural peptides and are not suitable for designing target-specific binders with improved pharmaceutical properties, such as macrocyclic peptides. Here we report a general framework that leverages the computational power of Rosetta for large-scale backbone sampling and energy scoring, followed by side-chain composition, to design heterochiral cyclic peptides that bind to a protein surface of interest. To showcase the applicability of our approach, we identified two peptides (PD-i3 and PD-i6) that target PD-1, a key immune checkpoint, and work as protein ligand decoys. A comprehensive biophysical evaluation confirmed their binding mechanism to PD-1 and their inhibitory effect on the PD-1/PD-L1 interaction. Finally, elucidation of their solution structures by NMR served as validation of our de novo design approach. We anticipate that our results will provide a general framework for designing target-specific drug-like peptides.

Download Full-text