Hexameric Supramolecular Scaffold Orients Carbohydrates To Sense Bacteria

Metadata Label Value
Author(s) Grunstein, Dan, Maglinao, Maha, Kikkeri, Raghavendra, Collot, Mayeul, Barylyuk, Konstantin, Lepenies, Bernd, Kamena, Faustin, Zenobi, Renato, Seeberger, Peter H.
Publication Type Journal Items, Publication Status: Published
Full Text Search SFX for a Full-Text version of this document
Import to Mendeley Log in to provide feedback

Detailed Information

Metadata Field Content
Title Hexameric Supramolecular Scaffold Orients Carbohydrates To Sense Bacteria
Author(s) Grunstein, Dan
Maglinao, Maha
Kikkeri, Raghavendra
Collot, Mayeul
Barylyuk, Konstantin
Lepenies, Bernd
Kamena, Faustin
Zenobi, Renato
Seeberger, Peter H.
Journal or Series Title Journal of the American Chemical Society
Volume Number 133
Issue Number 35
Start Page 13957
End Page 13966
ISSN 0002-7863
Publisher American Chemical Society
Publication Place Washington, DC
Publication Date 2011
Abstract Carbohydrates are integral to biological signaling networks and cell-cell interactions, yet the detection of discrete carbohydrate-lectin interactions remains difficult since binding is generally weak. A strategy to overcome this problem is to create multivalent sensors, where the avidity rather than the affinity of the interaction is important. Here we describe the development of a series of multivalent sensors that self-assemble via hydrophobic supramolecular interactions. The multivalent sensors are comprised of a fluorescent ruthenium(II) core surrounded by a heptarnannosylated beta-cyclodextrin scaffold. Two additional series of complexes were synthesized as proof-of-principle for supramolecular self-assembly, the fluorescent core alone and the core plus beta-cydodextrin. Spectroscopic analyses confirmed that the three mannosylated sensors displayed 14, 28, and 42 sugar units, respectively. Each complex adopted original and unique spatial arrangements. The sensors were used to investigate the influence of carbohydrate spatial arrangement and clustering on the mechanistic and qualitative properties of lectin binding. Simple visualization of binding between a fluorescent, multivalent mannose complex and the Escherichia coli strain ORN178 that possesses mannose-specific receptor sites illustrates the potential for these complexes as biosensors.
DOI 10.1021/ja2036767
Additional Notes Received 21 April 2011, Published 26 July 2011
Document Type Article
Publication Status Published
Language English
Assigned Organisational Unit(s) 03430
Organisational Unit(s)
NEBIS System Number 000019691
Source Database ID WOS-000295241400049
Description File Name MIME Type Size
No details could be found
There are no links available for this record.
This record has not been viewed during this period

  author = "Grunstein, Dan and Maglinao, Maha and Kikkeri, Raghavendra and Collot, Mayeul and Barylyuk, Konstantin and Lepenies, Bernd and Kamena, Faustin and Zenobi, Renato and Seeberger, Peter H.",
  title = "{H}exameric {S}upramolecular {S}caffold {O}rients {C}arbohydrates {T}o {S}ense {B}acteria",
  journal = "Journal of the American Chemical Society",
  year = 2011,
  volume = "133",
  number = "35",
  pages = "13957--13966",

E-Citations record created: Mon, 21 Nov 2011, 09:19:17 CET