Investigation of molecular interactions insight into some biologically active amino acids and aqueous solutions of an anti-malarial drug by physicochemical and theoretical approach

2021 ◽  
pp. 116933
Author(s):  
Modhusudan Mondal ◽  
Shatarupa Basak ◽  
Subhankar Choudhury ◽  
Narendra Nath Ghosh ◽  
Mahendra Nath Roy
Keyword(s):  
Amino Acids ◽  
Aqueous Solutions ◽  
Molecular Interactions ◽  
Theoretical Approach ◽  
Biologically Active ◽  
Insight Into

Molecular interactions of α-amino acids insight into aqueous β-cyclodextrin systems

Amino Acids ◽  
2013 ◽  
Vol 45 (4) ◽  
pp. 755-777 ◽  
Author(s):  
Deepak Ekka ◽  
Mahendra Nath Roy
Keyword(s):  
Amino Acids ◽  
Molecular Interactions ◽  
Insight Into

scholarly journals High-pressure investigations of solubility

2007 ◽  
Vol 79 (5) ◽  
pp. 861-874 ◽  
Author(s):  
Seiji Sawamura
Keyword(s):  
Amino Acids ◽  
High Pressure ◽  
Aqueous Solutions ◽  
Organic Compounds ◽  
High Pressures ◽  
Hydrophobic Hydration ◽  
Insight Into ◽  
Inorganic And Organic

We have measured the solubilities of several inorganic and organic compounds at high pressures up to 400 MPa. For this purpose, care should be exercised in instrumentation. The results include solubility values for aqueous solutions of NaCl, NaCl.2H2O, toluene, anthracene, phenanthrene, and amino acids (Gly, Ala, Val, Leu, and Ile). In addition, we determined the solubility of C60 in n-hexane and toluene. The data for individual systems served to elucidate the mechanisms of dissolution. For example, the data for toluene, anthracene, and phenanthrene in water provided insight into hydrophobic hydration.

Imaging polymers, proteins and dna in aqueous solutions with the atomic force microscope

1989 ◽  
Vol 47 ◽  
pp. 32-33
Author(s):  
S.A.C. Gould ◽  
B. Drake ◽  
C.B. Prater ◽  
A.L. Weisenhorn ◽  
S.M. Lindsay ◽  
...  
Keyword(s):  
Amino Acids ◽  
Dna Sequencing ◽  
Aqueous Solutions ◽  
Atomic Force Microscope ◽  
Piezoelectric Crystal ◽  
Atomic Force ◽  
Structure Of Molecules ◽  
Optical Lever

The atomic force microscope (AFM) is an instrument that can be used to image many samples of interest in biology and medicine. Images of polymerized amino acids, polyalanine and polyphenylalanine demonstrate the potential of the AFM for revealing the structure of molecules. Images of the protein fibrinogen which agree with TEM images demonstrate that the AFM can provide topographical data on larger molecules. Finally, images of DNA suggest the AFM may soon provide an easier and faster technique for DNA sequencing.The AFM consists of a microfabricated SiO2 triangular shaped cantilever with a diamond tip affixed at the elbow to act as a probe. The sample is mounted on a electronically driven piezoelectric crystal. It is then placed in contact with the tip and scanned. The topography of the surface causes minute deflections in the 100 μm long cantilever which are detected using an optical lever.

scholarly journals Reconstitution in Proteoliposomes of the Recombinant Human Riboflavin Transporter 2 (SLC52A2) Overexpressed in E. coli

2019 ◽  
Vol 20 (18) ◽  
pp. 4416 ◽  
Author(s):  
Lara Console ◽  
Maria Tolomeo ◽  
Matilde Colella ◽  
Maria Barile ◽  
Cesare Indiveri
Keyword(s):  
Cardiovascular Disease ◽  
Amino Acids ◽  
Risk Factor ◽  
Biologically Active ◽  
Suitable Model ◽  
Native Protein ◽  
E Coli ◽  
Few Data ◽  
Riboflavin Transport

Background: the SLC52A2 gene encodes for the riboflavin transporter 2 (RFVT2). This transporter is ubiquitously expressed. It mediates the transport of Riboflavin across cell membranes. Riboflavin plays a crucial role in cells since its biologically active forms, FMN and FAD, are essential for the metabolism of carbohydrates, amino acids, and lipids. Mutation of the Riboflavin transporters is a risk factor for anemia, cancer, cardiovascular disease, neurodegeneration. Inborn mutations of SLC52A2 are associated with Brown-Vialetto-van Laere syndrome, a rare neurological disorder characterized by infancy onset. In spite of the important metabolic and physio/pathological role of this transporter few data are available on its function and regulation. Methods: the human recombinant RFVT2 has been overexpressed in E. coli, purified and reconstituted into proteoliposomes in order to characterize its activity following the [3H]Riboflavin transport. Results: the recombinant hRFVT2 showed a Km of 0.26 ± 0.07 µM and was inhibited by lumiflavin, FMN and Mg2+. The Riboflavin uptake was also regulated by Ca2+. The native protein extracted from fibroblast and reconstituted in proteoliposomes also showed inhibition by FMN and lumiflavin. Conclusions: proteoliposomes represent a suitable model to assay the RFVT2 function. It will be useful for screening the mutation of RFVT2.

Volatile Anesthetics Affect Nutrient Availability in Yeast

Genetics ◽  
2002 ◽  
Vol 161 (2) ◽  
pp. 563-574
Author(s):  
Laura K Palmer ◽  
Darren Wolfe ◽  
Jessica L Keeley ◽  
Ralph L Keil
Keyword(s):  
Amino Acids ◽  
Nutrient Availability ◽  
Wild Type Strain ◽  
Volatile Anesthetic ◽  
Volatile Anesthetics ◽  
Wild Type ◽  
Anesthetic Exposure ◽  
Sites Of Action ◽  
Insight Into ◽  
Lines Of Evidence

Abstract Volatile anesthetics affect all cells and tissues tested, but their mechanisms and sites of action remain unknown. To gain insight into the cellular activities of anesthetics, we have isolated genes that, when overexpressed, render Saccharomyces cerevisiae resistant to the volatile anesthetic isoflurane. One of these genes, WAK3/TAT1, encodes a permease that transports amino acids including leucine and tryptophan, for which our wild-type strain is auxotrophic. This suggests that availability of amino acids may play a key role in anesthetic response. Multiple lines of evidence support this proposal: (i) Deletion or overexpression of permeases that transport leucine and/or tryptophan alters anesthetic response; (ii) prototrophic strains are anesthetic resistant; (iii) altered concentrations of leucine and tryptophan in the medium affect anesthetic response; and (iv) uptake of leucine and tryptophan is inhibited during anesthetic exposure. Not all amino acids are critical for this response since we find that overexpression of the lysine permease does not affect anesthetic sensitivity. These findings are consistent with models in which anesthetics have a physiologically important effect on availability of specific amino acids by altering function of their permeases. In addition, we show that there is a relationship between nutrient availability and ubiquitin metabolism in this response.

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