Synthetic Strategy for Rational Design of Single-Chain Magnets

2005 ◽  
Vol 78 (10) ◽  
pp. 1725-1748 ◽  
Author(s):  
Hitoshi Miyasaka ◽  
Rodolphe Clérac
Keyword(s):  
Rational Design ◽  
Single Chain ◽  
Synthetic Strategy ◽  
Single Chain Magnets

Crystal engineering to control the magnetic interaction between weak ferromagnetic single-chain magnets assembled in a 3D framework

2016 ◽  
Vol 52 (56) ◽  
pp. 8722-8725 ◽  
Author(s):  
Lei Su ◽  
Wei-Chao Song ◽  
Jiong-Peng Zhao ◽  
Fu-Chen Liu
Keyword(s):  
Crystal Engineering ◽  
Magnetic Interaction ◽  
High Dimensional ◽  
Single Chain ◽  
Synthetic Strategy ◽  
Dimensional Network ◽  
3D Framework ◽  
Single Chain Magnets ◽  
Weak Ferromagnetic

A synthetic strategy of control of the arrangement and the magnetism of the SCMs by assembly of the chains into a high dimensional network was illustrated in a family of a weak antiferromagnetic chain based 3D framework.

scholarly journals Computational and Rational Design of Single-Chain Antibody against Tick-Borne Encephalitis Virus for Modifying Its Specificity

Viruses ◽  
2021 ◽  
Vol 13 (8) ◽  
pp. 1494
Author(s):  
Ivan K. Baykov ◽  
Pavel Y. Desyukevich ◽  
Ekaterina E. Mikhaylova ◽  
Olga M. Kurchenko ◽  
Nina V. Tikunova
Keyword(s):  
Rational Design ◽  
Fold Increase ◽  
Encephalitis Virus ◽  
Chimeric Antibody ◽  
Single Chain ◽  
Single Chain Antibody ◽  
Glycoprotein E ◽  
Tick Borne Encephalitis ◽  
Tick Borne Encephalitis Virus ◽  
Far Eastern

Tick-borne encephalitis virus (TBEV) causes 5−7 thousand cases of human meningitis and encephalitis annually. The neutralizing and protective antibody ch14D5 is a potential therapeutic agent. This antibody exhibits a high affinity for binding with the D3 domain of the glycoprotein E of the Far Eastern subtype of the virus, but a lower affinity for the D3 domains of the Siberian and European subtypes. In this study, a 2.2-fold increase in the affinity of single-chain antibody sc14D5 to D3 proteins of the Siberian and European subtypes of the virus was achieved using rational design and computational modeling. This improvement can be further enhanced in the case of the bivalent binding of the full-length chimeric antibody containing the identified mutation.

Sterically-induced synthesis of 3d–4f one-dimensional compounds: A new route towards 3d–4f single chain magnets

2008 ◽  
Vol 361 (14-15) ◽  
pp. 3997-4003 ◽  
Author(s):  
G. Calvez ◽  
K. Bernot ◽  
O. Guillou ◽  
C. Daiguebonne ◽  
A. Caneschi ◽  
...  
Keyword(s):  
Single Chain ◽  
One Dimensional ◽  
Sterically Induced ◽  
Single Chain Magnets

scholarly journals An antibody that prevents serpin polymerisation acts by inducing a novel allosteric behaviour

2016 ◽  
Vol 473 (19) ◽  
pp. 3269-3290 ◽  
Author(s):  
Neda Motamedi-Shad ◽  
Alistair M. Jagger ◽  
Maximilian Liedtke ◽  
Sarah V. Faull ◽  
Arjun Scott Nanda ◽  
...  
Keyword(s):  
Rational Design ◽  
Conformational Transition ◽  
Structural Basis ◽  
Linear Polymers ◽  
Single Chain ◽  
Opposite Face ◽  
Induced Changes ◽  
Β Sheet ◽  
Chain Form ◽  
Antiprotease Activity

Serpins are important regulators of proteolytic pathways with an antiprotease activity that involves a conformational transition from a metastable to a hyperstable state. Certain mutations permit the transition to occur in the absence of a protease; when associated with an intermolecular interaction, this yields linear polymers of hyperstable serpin molecules, which accumulate at the site of synthesis. This is the basis of many pathologies termed the serpinopathies. We have previously identified a monoclonal antibody (mAb4B12) that, in single-chain form, blocks α1-antitrypsin (α1-AT) polymerisation in cells. Here, we describe the structural basis for this activity. The mAb4B12 epitope was found to encompass residues Glu32, Glu39 and His43 on helix A and Leu306 on helix I. This is not a region typically associated with the serpin mechanism of conformational change, and correspondingly the epitope was present in all tested structural forms of the protein. Antibody binding rendered β-sheet A — on the opposite face of the molecule — more liable to adopt an ‘open’ state, mediated by changes distal to the breach region and proximal to helix F. The allosteric propagation of induced changes through the molecule was evidenced by an increased rate of peptide incorporation and destabilisation of a preformed serpin–enzyme complex following mAb4B12 binding. These data suggest that prematurely shifting the β-sheet A equilibrium towards the ‘open’ state out of sequence with other changes suppresses polymer formation. This work identifies a region potentially exploitable for a rational design of ligands that is able to dynamically influence α1-AT polymerisation.

Design of single chain magnets through cyanide-bearing six-coordinate complexes

2005 ◽  
Vol 249 (23) ◽  
pp. 2691-2729 ◽  
Author(s):  
Rodrigue Lescouëzec ◽  
Luminita Marilena Toma ◽  
Jacqueline Vaissermann ◽  
Michel Verdaguer ◽  
Fernando S. Delgado ◽  
...  
Keyword(s):  
Single Chain ◽  
Single Chain Magnets

Polyoxometalate-Assisted Assembly of Pearl-Chain-Like Cyanide-Bridged Single-Chain Magnets

2021 ◽  
Author(s):  
Zi-Yi Chen ◽  
Yue Cheng ◽  
Qi Liu ◽  
Yi-Fei Deng ◽  
Yuan-Zhu Zhang
Keyword(s):  
Single Chain ◽  
Single Chain Magnets

Elucidation of the paratope of scFv-8H9D4, a PAI-1 neutralizing antibody derivative

2003 ◽  
Vol 89 (01) ◽  
pp. 74-82 ◽  
Author(s):  
Koen Verbeke ◽  
Ann Gils ◽  
Jean-Marie Stassen ◽  
Paul Declerck
Keyword(s):  
Rational Design ◽  
Three Dimensional ◽  
Neutralizing Antibody ◽  
Plasminogen Activator Inhibitor ◽  
Site Directed Mutagenesis ◽  
Dimensional Structure ◽  
Single Chain ◽  
Plasminogen Activator Inhibitor 1 ◽  
Activator Inhibitor ◽  
Pai 1

SummaryInterfering with increased levels of plasminogen activator inhibitor-1 (PAI-1) might offer new therapeutic strategies for a variety of cardiovascular diseases. Inactivation of PAI-1 can be accomplished by a number of monoclonal antibodies (MA), including MA-8H9D4. In a previous study, a single-chain variable fragment (scFv-8H9D4) was cloned and found to have the same properties as the parental MA-8H9D4. In the present study, we identified the residues of scFv-8H9D4 that contribute significantly to the paratope. The complementarity determining region 3 from the heavy (H3) and the light (L3) chain were analysed through site-directed mutagenesis. Out of twelve mutations, only four residues appeared to contribute to the paratope. The affinity of scFv-8H9D4-H3-L97D for PAI-1 was 38-fold decreased (KA = 4.8 ± 0.2 × 107 M–1 vs. 1.8 ± 0.7 × 109 M–1 for scFv-8H9D4) whereas scFv-8H9D4-H3-R98Y did not bind to PAI-1. The affinities of scFv-8H9D4-L3-Y91S and scFv-8H9D4-L3-F94D for PAI-1 were 9- and 5-fold reduced, respectively, whereas the combined mutation resulted in an 86-fold decreased affinity (KA = 2.1 ± 0.2 × 107 M–1).In accordance with the affinity data, these mutants had no, or a reduced, PAI-1 inhibitory capacity, confirming that these four particular residues form the major interaction site of scFv-8H9D4 with PAI-1. In combination with the three-dimensional structure, these data contribute to the rational design of PAI-1 neutralizing compounds.

Single chain magnets: where to from here?

2008 ◽  
Vol 18 (40) ◽  
pp. 4750 ◽  
Author(s):  
Lapo Bogani ◽  
Alessandro Vindigni ◽  
Roberta Sessoli ◽  
Dante Gatteschi
Keyword(s):  
Single Chain ◽  
Single Chain Magnets

Cobalt(II)-Copper(II) Bimetallic Chains as a New Class of Single-Chain Magnets

2004 ◽  
Vol 16 (18) ◽  
pp. 1597-1600 ◽  
Author(s):  
E. Pardo ◽  
R. Ruiz-García ◽  
F. Lloret ◽  
J. Faus ◽  
M. Julve ◽  
...  
Keyword(s):  
Single Chain ◽  
New Class ◽  
Single Chain Magnets
Sign in / Sign up

Export Citation Format

Share Document