Circular dichroism of oligosaccharides containing N-acetyl amino sugars

Coduti, Phillip L.; Gordon, Eric C.; Bush, C. Allen

doi:10.1016/0003-2697(77)90003-3

Cited by 37 publications

(10 citation statements)

References 14 publications

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“…The larger vicinal coupling constants were observed for N'H and N2H protons, indicating that these amide protons are almost trans to their respective sugar ring protons. This is in good agreement with the data for acetamide sugars (19) The yields of the glycopeptides in the above glycosylation were about 20% for these glycopeptides. The peptides and the glycopeptides were identified by thin-layer chromatography and ' H-n.m.r.…”

Section: Dagsupporting

confidence: 91%

Conformational study of glycopeptides

Ishii

Inoue²,

Chûjô

1984

International Journal of Peptide and Protein Research

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The conformational feature has been studied by n.m.r. spectroscopy on the compounds, Boc‐Asn‐NHMe, Boc‐Asn‐Gly‐NHMe, Boc‐Gly‐Asn‐NHMe, and their glycosylated derivatives. From the temperature dependence of the amide proton chemical shifts and vicinal coupling constants, little change was confirmed in the peptide conformation upon N‐glycosylation. There is no particular intramolecular interaction between the peptide and carbohydrate moieties. Boc‐Asn‐Gly‐NHMe takes, to some extent, a folded structure with a hydrogen bond involving the amide proton of N‐methylamide group. This backbone conformation is also preferable in the corresponding glycopeptide.

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Section: Dagsupporting

confidence: 91%

Conformational study of glycopeptides

Ishii

Inoue²,

Chûjô

1984

International Journal of Peptide and Protein Research

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“…The spectrum of FcαRI Man9 is very similar, whereas FcαRI GlcNAc displays a shift of the minima, suggesting an alteration in the secondary structure. It has to be noted that also the lack of sugar moieties in the FcαRI GlcNAc can cause a slight shift in absorbance because carbohydrates themselves also represent a small CD signal (29).…”

Section: Resultsmentioning

confidence: 99%

Distinct Fcα receptor N-glycans modulate the binding affinity to immunoglobulin A (IgA) antibodies

Göritzer

Turupcu

Maresch

et al. 2019

Journal of Biological Chemistry

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Human immunoglobulin A (IgA) is the most prevalent antibody class at mucosal sites with an important role in mucosal defense. Little is known about the impact of N-glycan modifications of IgA1 and IgA2 on binding to the Fcα receptor (FcαRI), which is also heavily glycosylated at its extracellular domain. Here, we transiently expressed human epidermal growth factor receptor 2 (HER2)-binding monomeric IgA1, IgA2m(1), and IgA2m(2) variants in Nicotiana benthamiana ΔXT/FT plants lacking the enzymes responsible for generating nonhuman N-glycan structures. By coinfiltrating IgA with the respective glycan-modifying enzymes, we generated IgA carrying distinct homogenous N-glycans. We demonstrate that distinctly different N-glycan profiles did not influence antigen binding or the overall structure and integrity of the IgA antibodies but did affect their thermal stability. Using size-exclusion chromatography, differential scanning and isothermal titration calorimetry, surface plasmon resonance spectroscopy, and molecular modeling, we probed distinct IgA1 and IgA2 glycoforms for binding to four different FcαRI glycoforms and investigated the thermodynamics and kinetics of complex formation. Our results suggest that different N-glycans on the receptor significantly contribute to binding affinities for its cognate ligand. We also noted that full-length IgA and FcαRI form a mixture of 1:1 and 1:2 complexes tending toward a 1:1 stoichiometry due to different IgA tailpiece conformations that make it less likely that both binding sites are simultaneously occupied. In conclusion, N-glycans of human IgA do not affect its structure and integrity but its thermal stability, and FcαRI N-glycans significantly modulate binding affinity to IgA.

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“…In the Hamiltonian, the potential function is expanded as a polynomial in two dimensions V{r,R) = £ /^( 3) p-0q-0 to the required order to ensure a good representation of V(r,R) with regard to the electronic calculations.…”

Section: Vibrational Calculationsmentioning

confidence: 99%

Theoretical vibrational investigation of hydrogen-bonded complexes: application to hydrogen chloride...ammonia, hydrogen chloride...methylamine, and hydrogen bromide...ammonia

Bouteiller

Mijoule

Karpfen³

et al. 1987

J. Phys. Chem.

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Previously reported ab initio calculations at the SCF and SCF + Cl level are used for the infrared vibrational study of three closely related -•• (X = Cl, Br; Y = NH3, NH2CH3) hydrogen-bonded complexes. The force constants are computed up to the fourth order by means of a numerical procedure. A variational method, suitable in the case of strong coupling between two vibrations, is used to compute the vXH and i/XH.,Y stretching modes as well as the corresponding deuteriated modes for the three complexes.

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Circular dichroism of oligosaccharides containing N-acetyl amino sugars

Cited by 37 publications

References 14 publications

Conformational study of glycopeptides

Conformational study of glycopeptides

Distinct Fcα receptor N-glycans modulate the binding affinity to immunoglobulin A (IgA) antibodies

Theoretical vibrational investigation of hydrogen-bonded complexes: application to hydrogen chloride...ammonia, hydrogen chloride...methylamine, and hydrogen bromide...ammonia

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