Design of metal ion binding peptides

Biopolymers ◽  
1995 ◽  
Vol 37 (6) ◽  
pp. 401-410 ◽  
Author(s):  
R. Fattorusso ◽  
G. Morelli ◽  
A. Lombardi ◽  
F. Nastri ◽  
O. Maglio ◽  
...  
Keyword(s):  
Metal Ion ◽  
Ion Binding ◽  
Metal Ion Binding ◽  
Binding Peptides

Development of Metal Ion Binding Peptides Using Phage Surface Display Technology

2017 ◽  
Vol 262 ◽  
pp. 591-595 ◽  
Author(s):  
Nora Schönberger ◽  
Sabine Matys ◽  
Katrin Flemming ◽  
Falk Lehmann ◽  
Franziska L. Lederer ◽  
...  
Keyword(s):  
Metal Ion ◽  
Specific Binding ◽  
Surface Display ◽  
Ionic Species ◽  
Phage Display Library ◽  
Complexing Agents ◽  
Ion Binding ◽  
Metal Ion Binding ◽  
Display Technology ◽  
Binding Peptides

Phage surface display technology is a useful tool for the identification of biosorptive peptides. In this work it is used for the identification of cobalt, nickel and gallium binding peptides. We present methods for the enrichment of metal ion binding bacteriophage clones from a commercial phage display library. Metal ion selective peptides are suitable to separate as well as concentrate cobalt and nickel from copper black shale leaching products (EcoMetals project) and gallium from industrial waste waters (EcoGaIn project). In contrast to common capture methods of specific binding phage for solid materials the ionic species have to be immobilized prior to the bio-panning procedure. This was realized by chemical complexation of the metal ions using commercial complexing agents on porous matrices. Moreover, an option to harvest non elutable strong binding phage is proposed.

Metal-Ion-Binding Peptides: From Catalysis to Protein Tagging.

ChemInform ◽  
2003 ◽  
Vol 34 (49) ◽  
Author(s):  
Giulia Licini ◽  
Paolo Scrimin
Keyword(s):  
Metal Ion ◽  
Ion Binding ◽  
Metal Ion Binding ◽  
Binding Peptides ◽  
Protein Tagging

Identification of metal ion binding peptides containing unnatural amino acids by phage display

2013 ◽  
Vol 23 (9) ◽  
pp. 2598-2600 ◽  
Author(s):  
Jonathan W. Day ◽  
Chan Hyuk Kim ◽  
Vaughn V. Smider ◽  
Peter G. Schultz
Keyword(s):  
Amino Acids ◽  
Phage Display ◽  
Unnatural Amino Acids ◽  
Metal Ion ◽  
Ion Binding ◽  
Metal Ion Binding ◽  
Binding Peptides

Photophysical Characterisation, Metal Ion Binding and Enantiomeric Recognition of Chiral Ligands Containing Phenazine Fluorophore

2004 ◽  
Vol 69 (4) ◽  
pp. 885-896 ◽  
Author(s):  
Luisa Stella Dolci ◽  
Péter Huszthy ◽  
Erika Samu ◽  
Marco Montalti ◽  
Luca Prodi ◽  
...  
Keyword(s):  
Metal Ion ◽  
Photophysical Properties ◽  
Ion Binding ◽  
Metal Ion Binding ◽  
Ammonium Ions ◽  
Enantiomerically Pure ◽  
Binding Process ◽  
High Affinity ◽  
Enantiomeric Recognition ◽  
Chiral Species

Enantiomerically pure dimethyl- and diisobutyl-substituted phenazino-18-crown-6 ligands bind metal and ammonium ions and also primary aralkylammonium perchlorates in acetonitrile with high affinity, causing pronounced changes in their luminescence properties. In addition, they show enantioselectivity towards chiral primary aralkylammonium perchlorates. The possibility to monitor the binding process by photoluminescence spectroscopy can gain ground for the design of very efficient enantioselective chemosensors for chiral species. The observed changes in the photophysical properties are also an important tool for understanding the interactions present in the adduct.

scholarly journals Snapshots of a Non-Canonical RdRP in Action

Viruses ◽  
2021 ◽  
Vol 13 (7) ◽  
pp. 1260
Author(s):  
Diego S. Ferrero ◽  
Michela Falqui ◽  
Nuria Verdaguer
Keyword(s):  
Metal Ion ◽  
Rna Viruses ◽  
Ion Binding ◽  
Genome Replication ◽  
Metal Ion Binding ◽  
Insect Virus ◽  
X Ray ◽  
Template Strand ◽  
Nucleotide Incorporation ◽  
Elongation Process

RNA viruses typically encode their own RNA-dependent RNA polymerase (RdRP) to ensure genome replication and transcription. The closed “right hand” architecture of RdRPs encircles seven conserved structural motifs (A to G) that regulate the polymerization activity. The four palm motifs, arranged in the sequential order A to D, are common to all known template dependent polynucleotide polymerases, with motifs A and C containing the catalytic aspartic acid residues. Exceptions to this design have been reported in members of the Permutotetraviridae and Birnaviridae families of positive single stranded (+ss) and double-stranded (ds) RNA viruses, respectively. In these enzymes, motif C is located upstream of motif A, displaying a permuted C–A–B–D connectivity. Here we study the details of the replication elongation process in the non-canonical RdRP of the Thosea asigna virus (TaV), an insect virus from the Permutatetraviridae family. We report the X-ray structures of three replicative complexes of the TaV polymerase obtained with an RNA template-primer in the absence and in the presence of incoming rNTPs. The structures captured different replication events and allowed to define the critical interactions involved in: (i) the positioning of the acceptor base of the template strand, (ii) the positioning of the 3’-OH group of the primer nucleotide during RNA replication and (iii) the recognition and positioning of the incoming nucleotide. Structural comparisons unveiled a closure of the active site on the RNA template-primer binding, before rNTP entry. This conformational rearrangement that also includes the repositioning of the motif A aspartate for the catalytic reaction to take place is maintained on rNTP and metal ion binding and after nucleotide incorporation, before translocation.

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