Nanovesicles displaying functional linear and branched oligomannose self-assembled from sequence-defined Janus glycodendrimers.


Journal

Proceedings of the National Academy of Sciences of the United States of America
ISSN: 1091-6490
Titre abrégé: Proc Natl Acad Sci U S A
Pays: United States
ID NLM: 7505876

Informations de publication

Date de publication:
02 06 2020
Historique:
pubmed: 20 5 2020
medline: 18 8 2020
entrez: 20 5 2020
Statut: ppublish

Résumé

Cell surfaces are often decorated with glycoconjugates that contain linear and more complex symmetrically and asymmetrically branched carbohydrates essential for cellular recognition and communication processes. Mannose is one of the fundamental building blocks of glycans in many biological membranes. Moreover, oligomannoses are commonly found on the surface of pathogens such as bacteria and viruses as both glycolipids and glycoproteins. However, their mechanism of action is not well understood, even though this is of great potential interest for translational medicine. Sequence-defined amphiphilic Janus glycodendrimers containing simple mono- and disaccharides that mimic glycolipids are known to self-assemble into glycodendrimersomes, which in turn resemble the surface of a cell by encoding carbohydrate activity via supramolecular multivalency. The synthetic challenge of preparing Janus glycodendrimers containing more complex linear and branched glycans has so far prevented access to more realistic cell mimics. However, the present work reports the use of an isothiocyanate-amine "click"-like reaction between isothiocyanate-containing sequence-defined amphiphilic Janus dendrimers and either linear or branched oligosaccharides containing up to six monosaccharide units attached to a hydrophobic amino-pentyl linker, a construct not expected to assemble into glycodendrimersomes. Unexpectedly, these oligoMan-containing dendrimers, which have their hydrophobic linker connected via a thiourea group to the amphiphilic part of Janus glycodendrimers, self-organize into nanoscale glycodendrimersomes. Specifically, the mannose-binding lectins that best agglutinate glycodendrimersomes are those displaying hexamannose. Lamellar "raft-like" nanomorphologies on the surface of glycodendrimersomes, self-organized from these sequence-defined glycans, endow these membrane mimics with high biological activity.

Identifiants

pubmed: 32424105
pii: 2003938117
doi: 10.1073/pnas.2003938117
pmc: PMC7275670
doi:

Substances chimiques

Dendrimers 0
Glycoconjugates 0
Glycolipids 0
Isothiocyanates 0
Lectins 0
Oligosaccharides 0
Polysaccharides 0
Mannose PHA4727WTP

Types de publication

Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S.

Langues

eng

Sous-ensembles de citation

IM

Pagination

11931-11939

Informations de copyright

Copyright © 2020 the Author(s). Published by PNAS.

Déclaration de conflit d'intérêts

The authors declare no competing interest.

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Auteurs

Qi Xiao (Q)

Roy & Diana Vagelos Laboratories, Department of Chemistry, University of Pennsylvania, Philadelphia, PA 19104.
Institute of Computational Molecular Science, Temple University, Philadelphia, PA 19122.

Martina Delbianco (M)

Department of Biomolecular Systems, Max Planck Institute of Colloids and Interfaces, 14476 Potsdam, Germany.

Samuel E Sherman (SE)

Roy & Diana Vagelos Laboratories, Department of Chemistry, University of Pennsylvania, Philadelphia, PA 19104.

Aracelee M Reveron Perez (AM)

Roy & Diana Vagelos Laboratories, Department of Chemistry, University of Pennsylvania, Philadelphia, PA 19104.

Priya Bharate (P)

Department of Biomolecular Systems, Max Planck Institute of Colloids and Interfaces, 14476 Potsdam, Germany.

Alonso Pardo-Vargas (A)

Department of Biomolecular Systems, Max Planck Institute of Colloids and Interfaces, 14476 Potsdam, Germany.

Cesar Rodriguez-Emmenegger (C)

DWI - Leibniz Institute for Interactive Materials, 52074 Aachen, Germany.
Institute of Technical and Macromolecular Chemistry, RWTH Aachen University, 52074 Aachen, Germany.

Nina Yu Kostina (NY)

DWI - Leibniz Institute for Interactive Materials, 52074 Aachen, Germany.
Institute of Technical and Macromolecular Chemistry, RWTH Aachen University, 52074 Aachen, Germany.

Khosrow Rahimi (K)

DWI - Leibniz Institute for Interactive Materials, 52074 Aachen, Germany.
Institute of Technical and Macromolecular Chemistry, RWTH Aachen University, 52074 Aachen, Germany.

Dominik Söder (D)

DWI - Leibniz Institute for Interactive Materials, 52074 Aachen, Germany.
Institute of Technical and Macromolecular Chemistry, RWTH Aachen University, 52074 Aachen, Germany.

Martin Möller (M)

DWI - Leibniz Institute for Interactive Materials, 52074 Aachen, Germany.
Institute of Technical and Macromolecular Chemistry, RWTH Aachen University, 52074 Aachen, Germany.

Michael L Klein (ML)

Institute of Computational Molecular Science, Temple University, Philadelphia, PA 19122; mlklein@temple.edu peter.seeberger@mpikg.mpg.de percec@sas.upenn.edu.

Peter H Seeberger (PH)

Department of Biomolecular Systems, Max Planck Institute of Colloids and Interfaces, 14476 Potsdam, Germany; mlklein@temple.edu peter.seeberger@mpikg.mpg.de percec@sas.upenn.edu.
Institute of Chemistry and Biochemistry, Freie Universität Berlin, 14195 Berlin, Germany.

Virgil Percec (V)

Roy & Diana Vagelos Laboratories, Department of Chemistry, University of Pennsylvania, Philadelphia, PA 19104; mlklein@temple.edu peter.seeberger@mpikg.mpg.de percec@sas.upenn.edu.

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Classifications MeSH