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Mannose-binding analysis and biological application of pradimicins
Pradimicins (PRMs) are an exceptional family of natural products that specifically bind d-mannose (Man). In the past decade, their scientific significance has increased greatly, with the emergence of biological roles of Man-containing glycans. However, research into the use of PRMs has been severely...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The Japan Academy
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8795531/ https://www.ncbi.nlm.nih.gov/pubmed/35013028 http://dx.doi.org/10.2183/pjab.98.002 |
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author | NAKAGAWA, Yu ITO, Yukishige |
author_facet | NAKAGAWA, Yu ITO, Yukishige |
author_sort | NAKAGAWA, Yu |
collection | PubMed |
description | Pradimicins (PRMs) are an exceptional family of natural products that specifically bind d-mannose (Man). In the past decade, their scientific significance has increased greatly, with the emergence of biological roles of Man-containing glycans. However, research into the use of PRMs has been severely limited by their inherent tendency to form water-insoluble aggregates. Recently, we have established a derivatization strategy to suppress PRM aggregation, providing an opportunity for practical application of PRMs in glycobiological research. This article first outlines the challenges in studying Man-binding mechanisms and structural modifications of PRMs, and then describes our approach to address them. We also present our recent attempts toward the development of PRM-based research tools. |
format | Online Article Text |
id | pubmed-8795531 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | The Japan Academy |
record_format | MEDLINE/PubMed |
spelling | pubmed-87955312022-02-25 Mannose-binding analysis and biological application of pradimicins NAKAGAWA, Yu ITO, Yukishige Proc Jpn Acad Ser B Phys Biol Sci Review Pradimicins (PRMs) are an exceptional family of natural products that specifically bind d-mannose (Man). In the past decade, their scientific significance has increased greatly, with the emergence of biological roles of Man-containing glycans. However, research into the use of PRMs has been severely limited by their inherent tendency to form water-insoluble aggregates. Recently, we have established a derivatization strategy to suppress PRM aggregation, providing an opportunity for practical application of PRMs in glycobiological research. This article first outlines the challenges in studying Man-binding mechanisms and structural modifications of PRMs, and then describes our approach to address them. We also present our recent attempts toward the development of PRM-based research tools. The Japan Academy 2022-01-11 /pmc/articles/PMC8795531/ /pubmed/35013028 http://dx.doi.org/10.2183/pjab.98.002 Text en © 2022 The Author(s). https://creativecommons.org/licenses/by-nc/4.0/Published under the terms of the CC BY-NC license https://creativecommons.org/licenses/by-nc/4.0/. |
spellingShingle | Review NAKAGAWA, Yu ITO, Yukishige Mannose-binding analysis and biological application of pradimicins |
title | Mannose-binding analysis and biological application of pradimicins |
title_full | Mannose-binding analysis and biological application of pradimicins |
title_fullStr | Mannose-binding analysis and biological application of pradimicins |
title_full_unstemmed | Mannose-binding analysis and biological application of pradimicins |
title_short | Mannose-binding analysis and biological application of pradimicins |
title_sort | mannose-binding analysis and biological application of pradimicins |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8795531/ https://www.ncbi.nlm.nih.gov/pubmed/35013028 http://dx.doi.org/10.2183/pjab.98.002 |
work_keys_str_mv | AT nakagawayu mannosebindinganalysisandbiologicalapplicationofpradimicins AT itoyukishige mannosebindinganalysisandbiologicalapplicationofpradimicins |