Molecular Design of Specific Metal-Binding Peptide Sequences from Protein Fragments: Theory and Experiment

2008 ◽  
Vol 14 (26) ◽  
pp. 7836-7846 ◽  
Author(s):  
Milan Kožíšek ◽  
Aleš Svatoš ◽  
Miloš Buděšínský ◽  
Alexander Muck ◽  
Mikael C. Bauer ◽  
...  
Keyword(s):  
Metal Binding ◽  
Molecular Design ◽  
Binding Peptide ◽  
Protein Fragments ◽  
Specific Metal ◽  
Theory And Experiment

Quinoline- and isoquinoline-derived ligand design on TQEN (N,N,N′,N′-tetrakis(2-quinolylmethyl)ethylenediamine) platform for fluorescent sensing of specific metal ions and phosphate species

2020 ◽  
Vol 49 (48) ◽  
pp. 17494-17504 ◽  
Author(s):  
Yuji Mikata
Keyword(s):  
Metal Ions ◽  
Fluorescent Probes ◽  
Metal Binding ◽  
Ligand Design ◽  
Fluorescent Properties ◽  
Fluorescent Sensing ◽  
Phosphate Species ◽  
Specific Metal

Utilizing the unique metal-binding and fluorescent properties of methoxy-substituted (iso)quinolines, varieties of fluorescent probes were developed from TQEN (N,N,N′,N′-tetrakis(2-quinolylmethyl)ethylenediamine) structure.

scholarly journals Comparison of the sedimentation and gel-filtration behaviour of human apotransferrin and its copper and iron complexes

1973 ◽  
Vol 133 (4) ◽  
pp. 749-754 ◽  
Author(s):  
Peter A. Charlwood
Keyword(s):  
Metal Binding ◽  
Binding Sites ◽  
Equilibrium Dialysis ◽  
Gel Filtration ◽  
Sedimentation Velocity ◽  
Copper Binding ◽  
Metal Binding Sites ◽  
Stokes Radius ◽  
Effect Of Copper ◽  
Specific Metal

Equilibrium-dialysis experiments showed that Tris or citrate in the solution prevented copper from occupying completely the specific metal-binding sites on human transferrin. Differential measurements of sedimentation velocity under conditions where two atoms of copper per molecule of protein were bound showed an increase in s020,w, relative to that of the apoprotein, practically the same as that produced by two atoms of iron. Gel-filtration experiments made under the same conditions to investigate the effect of copper binding on the Stokes radius of the protein showed merely that it lost most of the metal as it passed down the column.

Contributions of cell wall and metal-binding peptide to Cd- and Cu-tolerances in suspension-cultured cells of tomato

1991 ◽  
Vol 104 (3) ◽  
pp. 217-229 ◽  
Author(s):  
Masahiro Inouhe ◽  
Madoka Mitsumune ◽  
Hiroshi Tohoyama ◽  
Masanori Joho ◽  
Tetsuo Murayama
Keyword(s):  
Cell Wall ◽  
Metal Binding ◽  
Cultured Cells ◽  
Binding Peptide ◽  
Suspension Cultured Cells

HEAVY-METAL INDUCED CHANGES IN NONPROTEINACEOUS THIOL LEVELS AND HEAVY-METAL BINDING PEPTIDE IN TETRASELMIS TETRATHELE (PRASINOPHYCEAE)

1999 ◽  
Vol 35 (5) ◽  
pp. 989-994 ◽  
Author(s):  
Masaya Satoh ◽  
Emi Karaki ◽  
Mamiko Kakehashi ◽  
Eisuke Okazaki ◽  
Toshio Gotoh ◽  
...  
Keyword(s):  
Heavy Metal ◽  
Metal Binding ◽  
Binding Peptide ◽  
Heavy Metal Binding ◽  
Induced Changes

Metal binding peptide inhibitors of vertebrate collagenase

1981 ◽  
Vol 101 (4) ◽  
pp. 1251-1258 ◽  
Author(s):  
Robert D. Gray ◽  
Hossain H. Saneii ◽  
Arno F. Spatola
Keyword(s):  
Metal Binding ◽  
Peptide Inhibitors ◽  
Binding Peptide ◽  
Vertebrate Collagenase

Study of complex formation with 2-hydroxyiminocarboxylates: specific metal binding ability of 2-(4-methylthiazol-2-yl)-2-(hydroxyimino)acetic acid

2002 ◽  
Vol 329 (1) ◽  
pp. 113-121 ◽  
Author(s):  
Andriy A Mokhir ◽  
Elzbieta Gumienna-Kontecka ◽  
Jolanta Świątek-Kozlowska ◽  
Elena G Petkova ◽  
Igor O Fritsky ◽  
...  
Keyword(s):  
Acetic Acid ◽  
Complex Formation ◽  
Metal Binding ◽  
Binding Ability ◽  
Specific Metal ◽  
Metal Binding Ability

Manganese and cobalt recovery by surface display of metal binding peptide on various loops of OmpC in Escherichia coli

2017 ◽  
Vol 45 (1) ◽  
pp. 31-41 ◽  
Author(s):  
Murali kannan Maruthamuthu ◽  
Vidhya Selvamani ◽  
Saravanan Prabhu Nadarajan ◽  
Hyungdon Yun ◽  
You-Kwan Oh ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Metal Binding ◽  
Surface Display ◽  
Binding Peptide ◽  
Cobalt Recovery

scholarly journals Tagging Retrovirus Vectors with a Metal Binding Peptide and One-Step Purification by Immobilized Metal Affinity Chromatography

2004 ◽  
Vol 78 (18) ◽  
pp. 9820-9827 ◽  
Author(s):  
Kaiming Ye ◽  
Sha Jin ◽  
Mohammad M. Ataai ◽  
Jerome S. Schultz ◽  
Jeanette Ibeh
Keyword(s):  
Affinity Chromatography ◽  
Metal Binding ◽  
Viral Vectors ◽  
Retroviral Vectors ◽  
Immobilized Metal Affinity Chromatography ◽  
Binding Peptide ◽  
Metal Affinity ◽  
Contaminant Level ◽  
Fold Reduction ◽  
One Step

ABSTRACT Retroviral vectors produced from packaging cells are invariably contaminated by protein, nucleic acid, and other substances introduced in the manufacturing process. Elimination of these contaminants from retroviral vector preparations is helpful to reduce unwanted side effects, and purified vector preparations are desirable to improve reproducibility of therapeutic effect. Here we report a novel approach to engineer a metal binding peptide (MBP)-tagged murine leukemia virus (MuLV), allowing for one-step purification of retroviral vectors by immobilized metal affinity chromatography (IMAC). We inserted a His6 peptide into an ecotropic envelope protein (Env) by replacing part of its hypervariable region sequence with a sequence encoding the His6 peptide. Display of the His6 tag on the surface of Env endowed the vectors with a high affinity for immobilized metal ions, such as nickel. We demonstrated that the His6-tagged MuLV could be produced to high titers and could be highly purified by one-step IMAC. The protein and DNA contaminants in the purified vector supernatants were below 7 μg/ml and 25 pg/ml, respectively, indicating a 1,229-fold reduction in protein contaminant level and a 6,800-fold reduction in DNA contaminant level. About 56% of the viral vectors were recovered in the IMAC purification. The purified vectors retained their functionality and infectivity. These results establish that an MBP can be functionally displayed on the surface of ecotropic retroviruses without interfering with their integrity, and MBP-tagged retroviral vectors can be highly purified by one-step IMAC.

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