[21] Mapping of hydrogen bonding between saccharides and proteins in solution

Glaudemans, Cornelis P.J.; Kòváč, Pavol; Nashed, E. M.

doi:10.1016/s0076-6879(94)47023-5

Cited by 16 publications

(5 citation statements)

References 24 publications

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“…Fluorinated carbohydrates are versatile carbohydrate mimetics used to probe or manipulate the recognition of carbohydrates by carbohydrate-binding proteins or carbohydrate-processing enzymes [1][2][3][4][5][6][7]. The introduction of additional fluorine atoms into a monofluorinated carbohydrate is an attractive way of modulating the binding affinity and pharmacokinetic properties of fluorinated glycomimetics.…”

Section: Introductionmentioning

confidence: 99%

Synthesis of multiply fluorinated N-acetyl-D-glucosamine and D-galactosamine analogs via the corresponding deoxyfluorinated glucosazide and galactosazide phenyl thioglycosides

Hamala¹,

Šťastná²,

Kurfiřt³

et al. 2021

Beilstein J. Org. Chem.

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Multiple fluorination of glycostructures has emerged as an attractive way of modulating their protein affinity, metabolic stability, and lipophilicity. Here we described the synthesis of a series of mono-, di- and trifluorinated N-acetyl-ᴅ-glucosamine and ᴅ-galactosamine analogs. The key intermediates are the corresponding multiply fluorinated glucosazide and galactosazide thioglycosides prepared from deoxyfluorinated 1,6-anhydro-2-azido-β-ᴅ-hexopyranose precursors by ring-opening reaction with phenyl trimethylsilyl sulfide. Nucleophilic deoxyfluorination at C4 and C6 by reaction with DAST, thioglycoside hydrolysis and azide/acetamide transformation completed the synthesis.

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Section: Introductionmentioning

confidence: 99%

Synthesis of multiply fluorinated N-acetyl-D-glucosamine and D-galactosamine analogs via the corresponding deoxyfluorinated glucosazide and galactosazide phenyl thioglycosides

Hamala¹,

Šťastná²,

Kurfiřt³

et al. 2021

Beilstein J. Org. Chem.

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“…Similar studies on other monoclonal antigalactan antibodies revealed the same subsite arrangement, while for the antidextran monoclonal immunoglobulin IgA W3129, the subsite affinities diminished in order of their location (Glaudemans, 1991;Glaudemans et al, 1994).…”

Section: Mapping Of Subsites Of Anticarbohydrate Antibodiesmentioning

confidence: 66%

“…The mapping of subsites of antigalactan and antidextran antibodies is an excellent example (Glaudemans, 1991;Glaudemans et al, 1994). The combining site of these antibodies can accommodate up to four sequentially linked monosaccharide residues, that is, it contains four subsites each binding a monosaccharide unit of the tetrasaccharide epitope.…”

Section: Mapping Of Subsites Of Anticarbohydrate Antibodiesmentioning

confidence: 99%

Analysis of Protein–Carbohydrate Interaction Using Engineered Ligands

Solı́s¹,

Dı́az-Mauriño²

1996

Glycosciences

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“…For the anti-galactan antibodies on the other hand, the negative standard entropy change of association continues to increase up to the pentasaccharide level. For the former case it was previously shown that the upstream (Pavliak et al, 1993) terminal glucopyranosyl residue of the homologous ␣(136)-gluco-oligosaccharides fits into a tight cavity-like pocket of the antibody with the penultimate glucosyl residue protruding from that pocket into the solution (Glaudemans et al, 1989(Glaudemans et al, , 1994a(Glaudemans et al, , 1994bNashed et al, 1990). On the other hand, for the anti-galactans the oligosaccharide hapten was shown to bind on the surface of the antibody combining area, with larger haptens making increasing linear contact (Glaudemans, 1987(Glaudemans, , 1991Glaudemans et al, 1984) with the antibody surface.…”

Section: Resultsmentioning

confidence: 99%

Observations on the Binding of Four Anti-carbohydrate Monoclonal Antibodies to Their Homologous Ligands

Nashed

Glaudemans

1996

Journal of Biological Chemistry

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The binding of four monoclonal immunoglobulins, two with specificity for beta(1-->6)-linked D-galactopyranans (IgA X24 and IgA J539) and two with specificity for the chain terminus of alpha(1-->6)-linked d-glucopyranans (IgA W3129 and IgA 16.4.12E), was measured with a number of their homologous oligosaccharide ligands at different temperatures. The results show a linear relationship between lnKa and 1/T, where Ka is the affinity constant and T is the absolute temperature. The unitary free energy of binding, DeltaGu, is virtually independent of T, and the DeltaSu is small when compared with DeltaGu. The enthalpy changes derived from van't Hoff plots are large and negative, indicating an exothermic binding effect, whereas the entropy changes are small and negative, indicating minor overall hydrophobic contributions. Measurements of the free energies of binding, in low and high salt buffers, of methyl beta-d-galactopyranoside and the methyl glycoside of beta(1-->6)-D-galactopyranotetraose with anti-galactan IgA X24 indicate that the monosaccharide has no hydrophobic interaction with the highest affinity subsite of IgA, whereas the tetraoside might have a modest hydrophobic interaction with the three other hapten-binding subsites of IgA. The standard entropy change of binding of the two groups (galactosyl and glucosyl) of oligosaccharides to the two respective sets (anti-galactan and anti-dextran) of antibodies shows a distinct, differing correlation with the hapten chain length within each set. This correlation agrees with the type of association previously established between the antibodies and either the interior determinants of the antigen (in the case of the anti-galactans) or the chain terminus (in the case of the anti-dextrans).

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[21] Mapping of hydrogen bonding between saccharides and proteins in solution

Cited by 16 publications

References 24 publications

Synthesis of multiply fluorinated N-acetyl-D-glucosamine and D-galactosamine analogs via the corresponding deoxyfluorinated glucosazide and galactosazide phenyl thioglycosides

Synthesis of multiply fluorinated N-acetyl-D-glucosamine and D-galactosamine analogs via the corresponding deoxyfluorinated glucosazide and galactosazide phenyl thioglycosides

Analysis of Protein–Carbohydrate Interaction Using Engineered Ligands

Observations on the Binding of Four Anti-carbohydrate Monoclonal Antibodies to Their Homologous Ligands

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