scholarly journals Behavior of ligand binding assays with crowded surfaces: Molecular model of antigen capture by antibody-conjugated nanoparticles

PLoS ONE ◽  
2017 ◽  
Vol 12 (9) ◽  
pp. e0185518 ◽  
Author(s):  
David C. Malaspina ◽  
Gabriel Longo ◽  
Igal Szleifer
Keyword(s):  
Ligand Binding ◽  
Molecular Model ◽  
Binding Assays ◽  
Antigen Capture

scholarly journals The structure of SeviL, a GM1b/asialo-GM1 binding R-type lectin from the mussel Mytilisepta virgata

2020 ◽  
Vol 10 (1) ◽  
Author(s):  
Kenichi Kamata ◽  
Kenji Mizutani ◽  
Katsuya Takahashi ◽  
Roberta Marchetti ◽  
Alba Silipo ◽  
...  
Keyword(s):  
Immune System ◽  
Sialic Acid ◽  
Ligand Binding ◽  
Steric Hindrance ◽  
Sequence Similarity ◽  
Binding Assays ◽  
Subunit Interface ◽  
Nmr Techniques ◽  
And Control ◽  
Asialo Gm1

AbstractSeviL is a recently isolated lectin found to bind to the linear saccharides of the ganglioside GM1b (Neu5Ac$$\alpha$$ α (2-3)Gal$$\beta$$ β (1-3)GalNAc$$\beta$$ β (1-4)Gal$$\beta$$ β (1-4)Glc) and its precursor, asialo-GM1 (Gal$$\beta$$ β (1-3)GalNAc$$\beta$$ β (1-4)Gal$$\beta$$ β (1-4)Glc). The crystal structures of recombinant SeviL have been determined in the presence and absence of ligand. The protein belongs to the $$\beta$$ β -trefoil family, but shows only weak sequence similarity to known structures. SeviL forms a dimer in solution, with one binding site per subunit, close to the subunit interface. Molecular details of glycan recognition by SeviL in solution were analysed by ligand- and protein-based NMR techniques as well as ligand binding assays. SeviL shows no interaction with GM1 due to steric hindrance with the sialic acid branch that is absent from GM1b. This unusual specificity makes SeviL of great interest for the detection and control of certain cancer cells, and cells of the immune system, that display asialo-GM1.

Characterization of labeled reagents in ligand-binding assays by a surface plasmon resonance biosensor

Bioanalysis ◽  
2017 ◽  
Vol 9 (2) ◽  
pp. 193-207 ◽  
Author(s):  
Jia Duo ◽  
JoAnne Bruno ◽  
Steven Piccoli ◽  
Binodh DeSilva ◽  
Yan J Zhang
Keyword(s):  
Surface Plasmon Resonance ◽  
Ligand Binding ◽  
Surface Plasmon ◽  
Plasmon Resonance ◽  
Binding Assays ◽  
Surface Plasmon Resonance Biosensor

scholarly journals The role of amino acid α38 in the control of oxygen binding to human adult and embryonic haemoglobin Portland

1999 ◽  
Vol 343 (3) ◽  
pp. 681-685 ◽  
Author(s):  
Tao ZHENG ◽  
Thomas BRITTAIN ◽  
Nicholas J. WATMOUGH ◽  
Roy E. WEBER
Keyword(s):  
Amino Acid ◽  
Ligand Binding ◽  
Significant Contribution ◽  
Molecular Model ◽  
Site Directed Mutagenesis ◽  
Oxygen Binding ◽  
Naturally Occurring ◽  
Two State Model ◽  
T State

The role of the amino acid at position α38 in haemoglobin has been probed using site-directed mutagenesis. When the Thr residue at position α38 (which is totally conserved in all mammals) is changed to a Gln, the equilibrium properties of the protein are significantly altered. Equilibrium and kinetic data show that the R-state properties of the protein are essentially unaffected by the mutation whilst the allosteric equilibrium and T-state properties are changed. Mutation of the naturally occurring Gln38 of the human embryonic haemoglobin ζ-chain (the only known non-Thr containing globin) to a Thr residue shows the converse change in properties produced by the adult mutation, although in this case the situation is complicated by significant chain heterogeneity in the T state. An extension of the two-state model of co-operativity is presented to describe quantitatively the equilibrium ligand binding in the presence of T-state chain heterogeneity. A molecular model is described in which the putative interaction of αGln38 and βTyr145 is identified which make a significant contribution to the previously reported unusual ligand-binding properties of the ζ-chain containing human embryonic haemoglobins.

Study of Cardiac Autonomic Receptors by Radiolabeled Ligand Binding Assays

1984 ◽  
pp. 77-94
Author(s):  
Allan S. Manalan ◽  
Larry R. Jones ◽  
Henry R. Besch ◽  
August M. Watanabe
Keyword(s):  
Ligand Binding ◽  
Binding Assays ◽  
Autonomic Receptors

Cell-Free Ligand Binding Assays for Nuclear Receptors

2003 ◽  
pp. 53-71 ◽  
Author(s):  
Stacey A Jones ◽  
Derek J Parks ◽  
Steven A Kliewer
Keyword(s):  
Ligand Binding ◽  
Nuclear Receptors ◽  
Free Ligand ◽  
Binding Assays

Considerations and rationale for the selection of LC-MS/MS or ligand binding assays for bioanalysis of therapeutic proteins

2016 ◽  
pp. 154-166
Author(s):  
Charles Scott Hottenstein ◽  
Eric Dobrzynski ◽  
Joshua Albert ◽  
Jonathan Kehler ◽  
Matthew Szapacs
Keyword(s):  
Ligand Binding ◽  
Therapeutic Proteins ◽  
Binding Assays ◽  
Selection Of

Ligand-binding assays with OBPs and CSPs

2020 ◽  
pp. 229-258 ◽  
Author(s):  
Chiara D'Onofrio ◽  
Valeriia Zaremska ◽  
Jiao Zhu ◽  
Wolfgang Knoll ◽  
Paolo Pelosi
Keyword(s):  
Ligand Binding ◽  
Binding Assays
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