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Hokkaido University Collection of Scholarly and Academic Papers >
Graduate School of Life Science / Faculty of Advanced Life Science >
Peer-reviewed Journal Articles, etc >
Altering the Modular Architecture of Galectins Affects its Binding with Synthetic a-Dystroglycan O-Mannosylated Core M1 Glycoconjugates In situ
| Title: | Altering the Modular Architecture of Galectins Affects its Binding with Synthetic a-Dystroglycan O-Mannosylated Core M1 Glycoconjugates In situ |
| Authors: | Villones Jr, Lareno L. L. Browse this author | | Ludwig, Anna-Kristin Browse this author | | Kikuchi, Seiya Browse this author | | Ochi, Rika Browse this author | | Nishimura, Shin-Ichiro Browse this author →KAKEN DB | | Gabius, Hans-Joachim Browse this author | | Kaltner, Herbert Browse this author | | Hinou, Hiroshi Browse this author →KAKEN DB |
| Keywords: | alpha-dystroglycan | | galectin | | laminin | | protein engineering |
| Issue Date: | 17-Jul-2023 |
| Publisher: | Wiley-Blackwell |
| Journal Title: | Chembiochem |
| Volume: | 24 |
| Issue: | 14 |
| Start Page: | e202200783 |
| Publisher DOI: | 10.1002/cbic.202200783 |
| Abstract: | The multifunctionality of galectins helps regulate a broad range of fundamental cellular processes via cis-binding and trans-bridging activities and has gained widespread attention with respect to the importance of the natural specificity/selectivity of this lectin family to its glycoconjugate receptors. Combining galectin (Gal)-1, -3, -4, and -9 variant test panels, achieved via rational protein engineering, and a synthetic a-dystroglycan (DG) O-Mannosylated core M1 glycopeptide library, a detailed comparative analysis was performed, utilizing microarray experiments to delineate the design-functionality relationships within this lectin family. Enhancement of prototype Gal-1 and chimera-type Gal-3 cis-binding toward the prepared ligands is possible by transforming these lectins into tandem-repeat type and prototypes, respectively. Furthermore, Gal-1 variants demonstrated improved trans-bridging capabilities between core M1 a-DG glycopeptides and laminins in microarray, suggesting the possible translational applications of these galectin variants in the treatment of some forms of a-dystroglycanopathy. |
| Rights: | This is the peer reviewed version of the following article : Altering the Modular Architecture of Galectins Affects its Binding with Synthetic a-Dystroglycan O-Mannosylated Core M1 Glycoconjugates In situ, which has been published in final form at https://doi.org/10.1002/cbic.202200783. This article may be used for non-commercial purposes in accordance with Wiley Terms and Conditions for Use of Self-Archived Versions. This article may not be enhanced, enriched or otherwise transformed into a derivative work, without express permission from Wiley or by statutory rights under applicable legislation. Copyright notices must not be removed, obscured or modified. The article must be linked to Wiley’s version of record on Wiley Online Library and any embedding, framing or otherwise making available the article or pages thereof by third parties from platforms, services and websites other than Wiley Online Library must be prohibited. |
| Type: | article (author version) |
| URI: | http://hdl.handle.net/2115/92805 |
| Appears in Collections: | 生命科学院・先端生命科学研究院 (Graduate School of Life Science / Faculty of Advanced Life Science) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)
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Submitter: 比能 洋
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