Continuous Injection Isothermal Titration Calorimetry for In Situ Evaluation of Thermodynamic Binding Properties of Ligand–Receptor Binding Models

2021 ◽  
Author(s):  
Ji Woong Chang ◽  
Antonios Armaou ◽  
Robert M. Rioux
Keyword(s):  
Isothermal Titration Calorimetry ◽  
Receptor Binding ◽  
Titration Calorimetry ◽  
Binding Properties ◽  
Binding Models ◽  
Continuous Injection

scholarly journals Formation of nanoparticles by cooperative inclusion between (S)-camptothecin-modified dextrans and β-cyclodextrin polymers

2015 ◽  
Vol 11 ◽  
pp. 147-154 ◽  
Author(s):  
Thorbjørn Terndrup Nielsen ◽  
Catherine Amiel ◽  
Laurent Duroux ◽  
Kim Lambertsen Larsen ◽  
Lars Wagner Städe ◽  
...  
Keyword(s):  
Aqueous Solution ◽  
Fluorescence Spectroscopy ◽  
Isothermal Titration Calorimetry ◽  
Degree Of Substitution ◽  
Titration Calorimetry ◽  
Binding Properties ◽  
High Binding ◽  
Cyclodextrin Polymers

Novel (S)-camptothecin–dextran polymers were obtained by “click” grafting of azide-modified (S)-camptothecin and alkyne-modified dextrans. Two series based on 10 kDa and 70 kDa dextrans were prepared with a degree of substitution of (S)-camptothecin between 3.1 and 10.2%. The binding properties with β-cyclodextrin and β-cyclodextrin polymers were measured by isothermal titration calorimetry and fluorescence spectroscopy, showing no binding with β-cyclodextrin but high binding with β-cyclodextrin polymers. In aqueous solution nanoparticles were formed from association between the (S)-camptothecin–dextran polymers and the β-cyclodextrin polymers.

scholarly journals A Comparative Study on Nickel Binding to Hpn-like Polypeptides from Two Helicobacter pylori Strains

2021 ◽  
Vol 22 (24) ◽  
pp. 13210
Author(s):  
Danuta Witkowska ◽  
Agnieszka Szebesczyk ◽  
Joanna Wątły ◽  
Michał Braczkowski ◽  
Magdalena Rowińska-Żyrek
Keyword(s):  
Helicobacter Pylori ◽  
Comparative Study ◽  
Potentiometric Titration ◽  
Isothermal Titration Calorimetry ◽  
Titration Calorimetry ◽  
Binding Properties ◽  
Protein Fragments ◽  
Nickel Binding ◽  
Independent Reaction

Combined potentiometric titration and isothermal titration calorimetry (ITC) methods were used to study the interactions of nickel(II) ions with the N-terminal fragments and histidine-rich fragments of Hpn-like protein from two Helicobacter pylori strains (11637 and 26695). The ITC measurements were performed at various temperatures and buffers in order to extract proton-independent reaction enthalpies of nickel binding to each of the studied protein fragments. We bring up the problem of ITC results of nickel binding to the Hpn-like protein being not always compatible with those from potentiometry and MS regarding the stoichiometry and affinity. The roles of the ATCUN motif and multiple His and Gln residues in Ni(II) binding are discussed. The results provided the possibility to compare the Ni(II) binding properties between N-terminal and histidine-rich part of Hpn-like protein and between N-terminal parts of two Hpn-like strains, which differ mainly in the number of glutamine residues.

scholarly journals Substrate binding properties of potato tuber ADP-glucose pyrophosphorylase as determined by isothermal titration calorimetry

FEBS Letters ◽  
2015 ◽  
Vol 589 (13) ◽  
pp. 1444-1449 ◽  
Author(s):  
Bilal Cakir ◽  
Aytug Tuncel ◽  
Abigail R. Green ◽  
Kaan Koper ◽  
Seon-Kap Hwang ◽  
...  
Keyword(s):  
Potato Tuber ◽  
Isothermal Titration Calorimetry ◽  
Substrate Binding ◽  
Titration Calorimetry ◽  
Binding Properties ◽  
Adp Glucose Pyrophosphorylase

scholarly journals Modeling of Multivalent Ligand-Receptor Binding Measured by kinITC

Computation ◽  
2019 ◽  
Vol 7 (3) ◽  
pp. 46
Author(s):  
Franziska Erlekam ◽  
Sinaida Igde ◽  
Susanna Röblitz ◽  
Laura Hartmann ◽  
Marcus Weber
Keyword(s):  
Protein Folding ◽  
Kinetic Parameters ◽  
Invariant Subspace ◽  
Isothermal Titration Calorimetry ◽  
Receptor Binding ◽  
Kinetic Data ◽  
Titration Calorimetry ◽  
Subspace Projection ◽  
Binding Process ◽  
Sequential Binding

In addition to the conventional Isothermal Titration Calorimetry (ITC), kinetic ITC (kinITC) not only gains thermodynamic information, but also kinetic data from a biochemical binding process. Moreover, kinITC gives insights into reactions consisting of two separate kinetic steps, such as protein folding or sequential binding processes. The ITC method alone cannot deliver kinetic parameters, especially not for multivalent bindings. This paper describes how to solve the problem using kinITC and an invariant subspace projection. The algorithm is tested for multivalent systems with different valencies.

scholarly journals Isothermal titration calorimetry as a complementary method for investigating nanoparticle–protein interactions

Nanoscale ◽  
2019 ◽  
Vol 11 (41) ◽  
pp. 19265-19273 ◽  
Author(s):  
Domenik Prozeller ◽  
Svenja Morsbach ◽  
Katharina Landfester
Keyword(s):  
Protein Adsorption ◽  
Thermodynamic Parameters ◽  
Intermolecular Interactions ◽  
Isothermal Titration Calorimetry ◽  
Protein Interactions ◽  
Titration Calorimetry ◽  
Complementary Technique ◽  
Complementary Method

Isothermal titration calorimetry (ITC) is a complementary technique that can be used for investigations of protein adsorption on nanomaterials, as it quantifies the thermodynamic parameters of intermolecular interactionsin situ.

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