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About:
Nanovesicles displaying functional linear and branched oligomannose self-assembled from sequence-defined Janus glycodendrimers
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wasabi.inria.fr
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Academic Article
research paper
schema:ScholarlyArticle
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type
Academic Article
research paper
schema:ScholarlyArticle
isDefinedBy
Covid-on-the-Web dataset
has title
Nanovesicles displaying functional linear and branched oligomannose self-assembled from sequence-defined Janus glycodendrimers
Creator
Klein, Michael
Xiao, Qi
Seeberger, Peter
Bharate, Priya
Delbianco, Martina
Kostina, Nina
Möller, Martin
Pardo-Vargas, Alonso
Percec, Virgil
Rahimi, Khosrow
Reveron Perez, Aracelee
Rodriguez-Emmenegger, Cesar
Sherman, Samuel
Soeder, Dominik
topic
covid:9a168e4aa554a6f77c6f34794ae9b17dac2d003f#this
Source
Medline; PMC
abstract
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.
has issue date
2020-06-02
(
xsd:dateTime
)
bibo:doi
10.1073/pnas.2003938117
bibo:pmid
32424105
has license
cc-by-nc-nd
sha1sum (hex)
9a168e4aa554a6f77c6f34794ae9b17dac2d003f
schema:url
https://doi.org/10.1073/pnas.2003938117
resource representing a document's title
Nanovesicles displaying functional linear and branched oligomannose self-assembled from sequence-defined Janus glycodendrimers
has PubMed Central identifier
PMC7275670
has PubMed identifier
32424105
schema:publication
Proc Natl Acad Sci U S A
resource representing a document's body
covid:9a168e4aa554a6f77c6f34794ae9b17dac2d003f#body_text
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http://vocab.deri.ie/void#inDataset
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https://covidontheweb.inria.fr:4443/about/id/http/ns.inria.fr/covid19/9a168e4aa554a6f77c6f34794ae9b17dac2d003f
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named entity 'E. Merck'
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named entity 'reaction vessel'
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named entity 'TMSOTf'
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named entity 'mmol'
named entity 'MnCl2'
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named entity 'Perkin-Elmer'
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