| |  Online-Ressource |
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| Verfasst von: | Beckwith, Donella M [VerfasserIn]  |
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| | FitzGerald, Forrest G. [VerfasserIn] |
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| | Rodriguez Benavente, Maria C. [VerfasserIn] |
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| | Mercer, Elizabeth R. [VerfasserIn] |
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| | Ludwig, Anna-Kristin [VerfasserIn] |
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| | Michalak, Malwina [VerfasserIn] |
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| | Kaltner, Herbert [VerfasserIn] |
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| | Kopitz, Jürgen [VerfasserIn] |
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| | Gabius, Hans-Joachim [VerfasserIn] |
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| | Cudic, Maré [VerfasserIn] |
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| Titel: | Calorimetric analysis of the interplay between synthetic Tn antigen-presenting MUC1 glycopeptides and human macrophage galactose-type lectin |
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| Verf.angabe: | Donella M. Beckwith, Forrest G. FitzGerald, Maria C. Rodriguez Benavente, Elizabeth R. Mercer, Anna-Kristin Ludwig, Malwina Michalak, Herbert Kaltner, Jürgen Kopitz, Hans-Joachim Gabius, and Maré Cudic |
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| E-Jahr: | 2021 |
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| Jahr: | February 9, 2021 |
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| Umfang: | 42 S. |
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| Teil: | volume:60 |
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| | year:2021 |
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| | number:7 |
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| | pages:547-588 |
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| | extent:42 |
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| Fussnoten: | Gesehen am 05.08.2021 |
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| Titel Quelle: | Enthalten in: Biochemistry |
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| Ort Quelle: | Columbus, Ohio : American Chemical Society, 1962 |
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| Jahr Quelle: | 2021 |
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| Band/Heft Quelle: | 60(2021), 7, Seite 547-588 |
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| ISSN Quelle: | 1520-4995 |
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| Abstract: | Human macrophage galactose-type lectin (hMGL, HML, CD301, CLEC10A), a C-type lectin expressed by dendritic cells and macrophages, is a receptor for N-acetylgalactosamine alpha-linked to serine/threonine residues (Tn antigen, CD175) and its alpha 2,6-sialylated derivative (sTn, CD175s). Because these two epitopes are among malignant cell glycan displays, particularly when presented by mucin-1 (MUC1), assessing the influence of the site and frequency of glycosylation on lectin recognition will identify determinants governing this interplay. Thus, chemical synthesis of the tandem-repeat O-glycan acceptor region of MUC1 and site-specific threonine glycosylation in all permutations were carried out. Isothermal titration calorimetry (ITC) analysis of the binding of hMGL to this library of MUC1 glycopeptides revealed an enthalpy-driven process and an affinity enhancement of an order of magnitude with an increasing glycan count from 6-8 mu M for monoglycosylated peptides to 0.6 mu M for triglycosylated peptide. ITC measurements performed in D2O permitted further exploration of the solvation dynamics during binding. A shift in enthalpy-entropy compensation and contact position-specific effects with the likely involvement of the peptide surroundings were detected. KinITC analysis revealed a prolonged lifetime of the lectin-glycan complex with increasing glycan valency and with a change in the solvent to D2O. |
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| DOI: | doi:10.1021/acs.biochem.0c00942 |
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| URL: | Bitte beachten Sie: Dies ist ein Bibliographieeintrag. Ein Volltextzugriff für Mitglieder der Universität besteht hier nur, falls für die entsprechende Zeitschrift/den entsprechenden Sammelband ein Abonnement besteht oder es sich um einen OpenAccess-Titel handelt.
Volltext: https://doi.org/10.1021/acs.biochem.0c00942 |
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| | DOI: https://doi.org/10.1021/acs.biochem.0c00942 |
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| Datenträger: | Online-Ressource |
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| Sprache: | eng |
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| K10plus-PPN: | 1765256119 |
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| Verknüpfungen: | → Zeitschrift |
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Calorimetric analysis of the interplay between synthetic Tn antigen-presenting MUC1 glycopeptides and human macrophage galactose-type lectin / Beckwith, Donella M [VerfasserIn]; February 9, 2021 (Online-Ressource)
