Carbohydrates in Chemistry and Biology 2000
DOI: 10.1002/9783527618255.ch31
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Protein‐Carbohydrate Interaction: Fundamental Considerations

Abstract: A major-if not the major-rationale for the study of carbohydrate chemistry derives from the roles played by glycoconjugates in biology [l]. In almost all such roles a carbohydrate ligand must bind to a protein receptor. There exists, then, tremendous potential to modulate biological activity through the creation of high affinity mimics of native saccharide receptors; such compounds have potential therapeutic value in the treatment of viral, parasitic, mycoplasmal and bacterial infections, and the treatment of … Show more

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Cited by 25 publications
(27 citation statements)
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“…For one of the aminoglycosides studied, amikacin, the affinity was too low to obtain accurate values for Δ H and T Δ S . All binding interactions were characterized by favorable enthalpy (−Δ H ) and unfavorable entropy (− T Δ S ), which is typical for carbohydrate−protein interactions ( ). The binding was tighter in the presence of MgAMPCPP for all aminoglycosides studied with the exception of sisomicin.…”
Section: Resultsmentioning
confidence: 99%
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“…For one of the aminoglycosides studied, amikacin, the affinity was too low to obtain accurate values for Δ H and T Δ S . All binding interactions were characterized by favorable enthalpy (−Δ H ) and unfavorable entropy (− T Δ S ), which is typical for carbohydrate−protein interactions ( ). The binding was tighter in the presence of MgAMPCPP for all aminoglycosides studied with the exception of sisomicin.…”
Section: Resultsmentioning
confidence: 99%
“…However, in the quaternary complex the entropy (T∆S) is more negative for kanamycin A, resulting in weaker binding for kanamycin A compared to kanamycin B. The ability of an amino group to form more hydrogen bonds than a hydroxyl group may explain the greater affinity for kanamycin B. Hydrogen bonds are the major interactions governing affinity and specificity in enzyme-carbohydrate interactions (22,23,25). The change from an amino to a hydroxyl group can alter the number and geometry of hydrogen bonds formed in the complex.…”
Section: ∆G ) -Rt Ln K Amentioning
confidence: 99%
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“…In particular, glycans are supposed to have considerable conformational flexibility, at least in their uncomplexed states. Therefore, carbohydrate-protein interactions generally involve the loss of conformational entropy, which significantly contributes to the free energy difference between the free and bound states of interaction systems [ 75 ]. The triantennary high-mannose-type oligosaccharides possess remarkable degrees of motional freedom; therefore, they occupy vast conformational spaces.…”
Section: Conformational Dynamics Of High-mannose-type Oligosaccharmentioning
confidence: 99%
“…These systems typically exhibit extreme enthalpy−entropy compensation, with very large unfavorable entropies of binding. ( 58 ) Over a decade ago, in seeking to rationalize this phenomenon, and on the basis of the extremely limited data that were available at the time, Lemieux proposed( 59 ) “At nonpolar surfaces...an organized layer of molecules is formed that, on being released to bulk, provides an increase in entropy. In contrast, the liberation of water molecules from polyamphiphilic surfaces causes important decreases in both Δ H and T Δ S ....” Given that this hypothesis has yet to find experimental support to the best of our knowledge, the present data suggest that an alternative explanation might entail the sequestration of solvent water molecules on complexation.…”
Section: Resultsmentioning
confidence: 99%