Mid- and Far-Infrared Marker Bands of the Metal Coordination Sites of the Histidine Side Chains in the Protein Cu,Zn-Superoxide Dismutase

2014 ◽  
Vol 2014 (27) ◽  
pp. 4650-4659 ◽  
Author(s):  
Bertrand Xerri ◽  
Hugo Petitjean ◽  
François Dupeyrat ◽  
Jean-Pierre Flament ◽  
Alain Lorphelin ◽  
...  
Keyword(s):  
Superoxide Dismutase ◽  
Far Infrared ◽  
Metal Coordination ◽  
Side Chains ◽  
Coordination Sites

Tetra- and Octalactam Macrocycles and Catenanes with Exocyclic Metal Coordination Sites: Versatile Building Blocks for Supramolecular Chemistry

2003 ◽  
Vol 9 (6) ◽  
pp. 1332-1347 ◽  
Author(s):  
Xi-you Li ◽  
Jens Illigen ◽  
Martin Nieger ◽  
Steffen Michel ◽  
Christoph A. Schalley
Keyword(s):  
Supramolecular Chemistry ◽  
Building Blocks ◽  
Metal Coordination ◽  
Coordination Sites

Construction of dimetal-containing dithiolene and Schiff base conjugated polymer coating: exploiting metal coordination as a design strategy for improving infrared stealth properties

2019 ◽  
Vol 10 (43) ◽  
pp. 5839-5848 ◽  
Author(s):  
Jingwen Cai ◽  
Jianhua Han ◽  
Guojia Ma ◽  
Xing Liu ◽  
Jinyan Wang ◽  
...  
Keyword(s):  
Schiff Base ◽  
Conjugated Polymer ◽  
Polymer Coating ◽  
Near Infrared ◽  
Far Infrared ◽  
Design Strategy ◽  
Polymer Coatings ◽  
Metal Coordination ◽  
Infrared Range

Dimetal-containing dithiolene and Schiff base conjugated polymer coatings are constructed and exhibit excellent stealth abilities in the NIR (near-infrared) and MFIR (mid–far-infrared) range.

Engineering metal coordination sites into the antibody light chain

1993 ◽  
Vol 115 (11) ◽  
pp. 4449-4456 ◽  
Author(s):  
Warren S. Wade ◽  
Jong S. Koh ◽  
Nianhe Han ◽  
Denise M. Hoekstra ◽  
Richard A. Lerner
Keyword(s):  
Light Chain ◽  
Metal Coordination ◽  
Coordination Sites

scholarly journals Lanthanide DO3A-Complexes Bearing Peptide Substrates: The Effect of Peptidic Side Chains on Metal Coordination and Relaxivity

Molecules ◽  
2021 ◽  
Vol 26 (8) ◽  
pp. 2176
Author(s):  
Sophie Laine ◽  
Jean-François Morfin ◽  
Mathieu Galibert ◽  
Vincent Aucagne ◽  
Célia S. Bonnet ◽  
...  
Keyword(s):  
Relaxation Dispersion ◽  
Metal Coordination ◽  
Side Chain ◽  
Side Chains ◽  
Potential Donor ◽  
Peptide Substrates ◽  
Amine Derivative ◽  
High Relaxivity ◽  
Hydrophilic Peptide ◽  
Nmrd Profiles

Two DO3A-type ligands conjugated to substrates of urokinase (L3) and caspase-3 (L4) via a propyl-amide linker were synthesized and their lanthanide(III) (Ln3+) complexes studied. A model compound without peptide substrate (L2) and an amine derivative ligand mimicking the state after enzymatic cleavage (L1) were also prepared. Proton Nuclear Magnetic Relaxation Dispersion (NMRD) profiles recorded on the gadolinium(III) (Gd3+) complexes, complemented with the assessment of hydration numbers via luminescence lifetime measurements on the Eu3+ analogues, allowed us to characterize the lanthanide coordination sphere in the chelates. These data suggest that the potential donor groups of the peptide side chains (carboxylate, amine) interfere in metal coordination, leading to non-hydrated LnL3 and LnL4 complexes. Nevertheless, GdL3 and GdL4 retain a relatively high relaxivity due to an important second-sphere contribution generated by the strongly hydrophilic peptide chain. Weak PARACEST effects are detected for the amine-derivative EuL1 and NdL1 chelates. Unfortunately, the GdL3 and GdL4 complexes are not significantly converted by the enzymes. The lack of enzymatic recognition of these complexes can likely be explained by the participation of donor groups from the peptide side chain in metal coordination.

Interaction of chemically modified tetracyclines with catalytic Zn(II) ion in matrix metalloproteinase: evidence for metal coordination sites

2011 ◽  
Vol 128 (3) ◽  
pp. 377-388 ◽  
Author(s):  
Bruna L. Marcial ◽  
Luiz Antônio S. Costa ◽  
Wagner B. De Almeida ◽  
Cleber P. A. Anconi ◽  
Hélio F. Dos Santos
Keyword(s):  
Matrix Metalloproteinase ◽  
Metal Coordination ◽  
Chemically Modified ◽  
Coordination Sites ◽  
Chemically Modified Tetracyclines
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