Thermodynamic Binding Parameters of Individual Epitopes of Multivalent Carbohydrates to Concanavalin A As Determined by “Reverse” Isothermal Titration Microcalorimetry†

Biochemistry ◽  
2002 ◽  
Vol 41 (4) ◽  
pp. 1359-1363 ◽  
Author(s):  
Tarun K. Dam ◽  
René Roy ◽  
Daniel Pagé ◽  
C. Fred Brewer
Keyword(s):  
Concanavalin A ◽  
Binding Parameters ◽  
Isothermal Titration Microcalorimetry ◽  
Titration Microcalorimetry

Complexation of β-Cyclodextrin with a Gemini Surfactant Studied by Isothermal Titration Microcalorimetry and Surface Tensiometry

Langmuir ◽  
2014 ◽  
Vol 30 (23) ◽  
pp. 6756-6762 ◽  
Author(s):  
Mária Benkő ◽  
László A. Király ◽  
Sándor Puskás ◽  
Zoltán Király
Keyword(s):  
Gemini Surfactant ◽  
Isothermal Titration Microcalorimetry ◽  
Titration Microcalorimetry ◽  
Surface Tensiometry

scholarly journals Effect of substituent on the thermodynamics of d-glucopyranoside binding to concanavalin A, pea (Pisum sativum) lectin and lentil (Lens culinaris) lectin

1996 ◽  
Vol 316 (1) ◽  
pp. 123-129 ◽  
Author(s):  
Frederick P. SCHWARZ ◽  
Sandra MISQUITH ◽  
Avadhesha SUROLIA
Keyword(s):  
Concanavalin A ◽  
Hydrophobic Interactions ◽  
Entropy Change ◽  
Titration Calorimetry ◽  
Binding Parameters ◽  
Surrounding Water ◽  
Pea Lectin ◽  
Lentil Lectin ◽  
Binding Enthalpy ◽  
Derivatives Of

Titration calorimetry measurements of the binding of phenyl-α (αPhOGlu), 3-methoxy (3MeOGlu), fluorodeoxy and deoxy derivatives of α-D-glucopyranose (Glu) to concanavalin A (conA), pea lectin and lentil lectin were performed at approx. 10 and 25 °C in 0.01 M dimethylglutaric acid/NaOH buffer, pH 6.9, containing 0.15 M NaCl and Mn2+ and Ca2+ ions. Apparently the 3-deoxy, 4-deoxy and 6-deoxy as well as the 4-fluorodeoxy and 6-fluorodeoxy derivatives of Glu do not bind to the lectins because no heat release was observed on the addition of aliquots of solutions of these derivatives to the lectin solutions. The binding enthalpies, ∆H0b, and entropies, ∆S0b, determined from the measurements were compared with the same thermodynamic binding parameters for Glu, D-mannopyranoside and methyl-α-D-glucopyranoside (αMeOGlu). The binding reactions are enthalpically driven with little change in the heat capacity on binding, and exhibit enthalpy–entropy compensation. Differences between the thermodynamic binding parameters can be rationalized in terms of the interactions apparent in the known crystal structures of the methyl-α-D-mannopyranoside-conA [Derewenda, Yariv, Helliwell, Kalb (Gilboa), Dodson, Papiz, Wan and Campbell (1989) EMBO J. 8, 2189–2193] and pea lectin-trimannopyranoside [Rini, Hardman, Einspahr, Suddath and Carber (1993) J. Biol. Chem. 268, 10126–10132] complexes. Increases in the entropy change on binding are observed for αMeOGlu binding to pea and lentil lectin, for αPhOGlu binding to conA and pea lectin, and for 3MeOGlu binding to pea lectin relative to the entropy change for Glu binding, and imply that the phenoxy and methoxy substituents provide additional hydrophobic interactions in the complex. Increases in the binding enthalpy relative to that of Glu are observed for deoxy and fluoro derivatives in the C-1 and C-2 positions and imply that these substituents weaken the interaction with the surrounding water, thereby strengthening the interaction with the binding site.

New Insights into Chitosan−DNA Interactions Using Isothermal Titration Microcalorimetry

2009 ◽  
Vol 10 (6) ◽  
pp. 1490-1499 ◽  
Author(s):  
Pei Lian Ma ◽  
Marc Lavertu ◽  
Françoise M. Winnik ◽  
Michael D. Buschmann
Keyword(s):  
Dna Interactions ◽  
Isothermal Titration Microcalorimetry ◽  
Titration Microcalorimetry

Direct Determination of Thiol pKaby Isothermal Titration Microcalorimetry

2004 ◽  
Vol 126 (34) ◽  
pp. 10508-10509 ◽  
Author(s):  
Stephen G. Tajc ◽  
Blanton S. Tolbert ◽  
Ravi Basavappa ◽  
Benjamin L. Miller
Keyword(s):  
Direct Determination ◽  
Isothermal Titration Microcalorimetry ◽  
Titration Microcalorimetry
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