Chemical Modification and Metal Binding Studies ofDatura innoxia

1996 ◽  
Vol 30 (1) ◽  
pp. 110-114 ◽  
Author(s):  
Lawrence R. Drake ◽  
Shan Lin ◽  
Gary D. Rayson ◽  
Paul J. Jackson
Keyword(s):  
Chemical Modification ◽  
Metal Binding ◽  
Binding Studies

Perspective on FTY720, an Immunosuppressant

Synthesis ◽  
2018 ◽  
Vol 50 (05) ◽  
pp. 968-983 ◽  
Author(s):  
Sivaraman Balasubramaniam ◽  
Ganapathy Sankaran ◽  
Sneh Badle
Keyword(s):  
Chemical Modification ◽  
Mode Of Action ◽  
Immunosuppressive Drugs ◽  
Binding Studies ◽  
Structure Activity Relationships ◽  
Structure Activity ◽  
Fingolimod Hydrochloride

FTY720 {fingolimod hydrochloride, 2-amino-2-[2-(4-octylphenyl)ethyl]propane-1,3-diol hydrochloride}, a novel immunosuppressant, was discovered by chemical modification based on the structure activity relationships of ISP-I (myriocin), a metabolite of the fungus Isaria­ sinclairii. This short perspective provides insights to the various strategies available in the literature for the synthesis of FTY720 and its analogues.1 Introduction2 Classification of Immunosuppressive Drugs3 The Rise of FTY7204 Different Synthetic Strategies for FTY7205 Analogues of FTY7206 Binding Studies of FTY7207 Mode of Action8 Conclusion

Synthesis and metal-binding studies of a novel pyrene discotic

2008 ◽  
Vol 49 (2) ◽  
pp. 238-242 ◽  
Author(s):  
Fadi M. Jradi ◽  
Mohammad H. Al-Sayah ◽  
Bilal R. Kaafarani
Keyword(s):  
Metal Binding ◽  
Binding Studies

The bacterial receptor protein, transferrin-binding protein B, does not independently facilitate the release of metal ion from human transferrin

2003 ◽  
Vol 81 (4) ◽  
pp. 275-283 ◽  
Author(s):  
Ulyana Nemish ◽  
Rong-Hua Yu ◽  
Leslie W Tari ◽  
Karla Krewulak ◽  
Anthony B Schryvers
Keyword(s):  
Outer Membrane ◽  
Metal Binding ◽  
Metal Ion ◽  
Binding Protein ◽  
Protein A ◽  
Nitrilotriacetic Acid ◽  
Receptor Protein ◽  
Binding Studies ◽  
Metal Ion Removal ◽  
Protein B

Pathogenic Gram-negative bacteria of the Pasteurellaceae and Neisseriaceae acquire iron for growth from host transferrin through the action of specific surface receptors. Iron is removed from transferrin by the receptor at the cell surface and is transported across the outer membrane to the periplasm. A periplasmic binding protein-dependent pathway subsequently transports iron into the cell. The transferrin receptor is composed of a largely surface-exposed lipoprotein, transferrin binding protein B, and a TonB-dependent integral outer membrane protein, transferrin binding protein A. To examine the role of transferrin binding protein B in the iron removal process, complexes of recombinant transferrin binding protein B and transferrin were prepared and compared with transferrin in metal-binding and -removal experiments. A polyhistidine-tagged form of recombinant transferrin binding protein B was able to purify a complex with transferrin that was largely monodisperse by dynamic light scattering analysis. Gallium was used instead of iron in the metal-binding studies, since it resulted in increased stability of recombinant transferrin binding protein B in the complex. Difference absorption spectra were used to monitor removal of gallium by nitrilotriacetic acid. Kinetic and equilibrium binding studies indicated that transferrin binds gallium more tightly in the presence of transferrin binding protein B. Thus, transferrin binding protein B does not facilitate metal ion removal and additional components are required for this process.Key words: iron, transport, outer membrane, lipoprotein, glycoprotein.

scholarly journals Metal-binding studies for a de novo designed calcium-binding protein

2002 ◽  
Vol 15 (7) ◽  
pp. 571-574 ◽  
Author(s):  
Anna L. Wilkins ◽  
Yiming Ye ◽  
Wei Yang ◽  
Hsiau-Wei Lee ◽  
Zhi-ren Liu ◽  
...  
Keyword(s):  
Metal Binding ◽  
Calcium Binding ◽  
De Novo ◽  
Binding Protein ◽  
Calcium Binding Protein ◽  
Binding Studies

scholarly journals Modification of Cys-837 identifies an actin-binding site in the beta-propeller protein scruin.

1997 ◽  
Vol 8 (3) ◽  
pp. 421-430 ◽  
Author(s):  
S Sun ◽  
M Footer ◽  
P Matsudaira
Keyword(s):  
Chemical Modification ◽  
Binding Site ◽  
Solvent Accessibility ◽  
The Other ◽  
Actin Binding ◽  
Binding Region ◽  
Binding Studies ◽  
Chemically Modified ◽  
Cross Links ◽  
Actin Binding Site

In the acrosomal process of Limulus sperm, the beta-propeller protein scruin cross-links actin into a crystalline bundle. To confirm that scruin has the topology of a beta-propeller protein and to understand how scruin binds actin, we compared the solvent accessibility of cysteine residues in scruin and the acrosomal process by chemical modification with (1,5-IAEDANS). In soluble scruin, the two most reactive cysteines of soluble scruin are C837 and C900, whereas C146, C333, and C683 are moderately reactive. This pattern of reactivity is consistent with the topology of a typical beta-propeller protein; all of the reactive cysteines map to putative loops and turns whereas the unreactive cysteines lie within the predicted interior of the protein. The chemical reactivities of cysteine in the acrosomal process implicate C837 at an actin-binding site. In contrast to soluble scruin, in the acrosomal process, C837 is completely unreactive while the other cysteines become less reactive. Binding studies of chemically modified scruin correlate the extent of modification at C837 with the extent of inhibition of actin binding. Furthermore, peptides corresponding to residues flanking C837 bind actin and narrow a possible actin-binding region to a KQK sequence. On the basis of these studies, our results suggest that an actin-binding site lies in the C-terminal domain of scruin and involves a putative loop defined by C837.

Use of phytofiltration technologies in the removal of heavy metals: A review

2004 ◽  
Vol 76 (4) ◽  
pp. 801-813 ◽  
Author(s):  
J. L. Gardea-Torresdey ◽  
G. de la Rosa ◽  
J. R. Peralta-Videa
Keyword(s):  
Chemical Modification ◽  
Adsorption Capacity ◽  
Metal Binding ◽  
Precious Metals ◽  
Spectroscopic Studies ◽  
Column Studies ◽  
Biosorption Process ◽  
Removal Of Heavy Metals ◽  
Aqueous Effluents ◽  
Amino Amide

Biosorption is a relatively new process that has proven very promising in the removal of contaminants from aqueous effluents. Microorganisms as well as plant- and animal-derived materials have been used as biosorbents by many researchers. Biomaterial immobilization and chemical modification improves the adsorption capacity and stability of biosorbents. Biosorption experiments over Cu(II), Cd(II), Pb(II), Cr(III), and Ni(II) demonstrated that biomass Cu(II) adsorption ranged from 8.09 to 45.9 mg g−1, while Cd(II) and Cr(VI) adsorption ranged from 0.4 to 10.8 mg g−1 and from 1.47 to 119 mg g−1, respectively. Mechanisms involved in the biosorption process include chemisorption, complexation, surface and pore adsorption-complexation, ion exchange, microprecipitation, hydroxide condensation onto the biosurface, and surface adsorption. Chemical modification and spectroscopic studies have shown that cellular components including carboxyl, hydroxyl, sulfate, sulfhydryl, phosphate, amino, amide, imine, and imidazol moieties have metal binding properties and are therefore the functional groups in the biomass. Column studies using support matrices for biomass immobilization such as silica, agar, polyacrilamide, polysulfone, alginates, cellulase, and different cross-linking agents have been performed to improve the biomass adsorption capacity and reusability. In this review, the salient features of plant-derived materials are highlighted as potential phytofiltration sources in the recovery of toxic heavy and precious metals.

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