Conformationally Constrained Functional Peptide Monolayers for the Controlled Display of Bioactive Carbohydrate Ligands (Articolo in rivista)

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  • Conformationally Constrained Functional Peptide Monolayers for the Controlled Display of Bioactive Carbohydrate Ligands (Articolo in rivista) (literal)
Anno
  • 2013-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1021/la4008894 (literal)
Alternative label
  • Kaplan J.M.; Shang J.; Gobbo P.; Antonello S.; Armelao L.; Chatare V.; Ratner D.M.; Andrade R.B.; Maran F. (2013)
    Conformationally Constrained Functional Peptide Monolayers for the Controlled Display of Bioactive Carbohydrate Ligands
    in Langmuir; ACS, American chemical society, Washington, DC (Stati Uniti d'America)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Kaplan J.M.; Shang J.; Gobbo P.; Antonello S.; Armelao L.; Chatare V.; Ratner D.M.; Andrade R.B.; Maran F. (literal)
Pagina inizio
  • 8187 (literal)
Pagina fine
  • 8192 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#url
  • http://pubs.acs.org/doi/abs/10.1021/la4008894 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 29 (literal)
Rivista
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo
  • 26 (literal)
Note
  • Scopu (literal)
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • 1,6,8,9 : Department of Chemistry, Temple University, Philadelphia, PA, United States / 2,7 : Department of Bioengineering, University of Washington, Seattle, WA, United States / 3,4,9 : Department of Chemistry, University of Padova, Padova, Italy / 5 : IENI-CNR, C/o Department of Chemistry, University of Padova, Padova, Italy (literal)
Titolo
  • Conformationally Constrained Functional Peptide Monolayers for the Controlled Display of Bioactive Carbohydrate Ligands (literal)
Abstract
  • In this study, we employed thiolated peptides of the conformationally constrained, strongly helicogenic ?-aminoisobutyric acid (Aib) residue to prepare self-assembled monolayers (SAMs) on gold surfaces. Electrochemistry and infrared reflection absorption spectroscopy support the formation of very well packed Aib-peptide SAMs. The immobilized peptides retain their helical structure, and the resulting SAMs are stabilized by a network of intermolecular H bonds involving the NH groups adjacent to the Au surface. Binary SAMs containing a synthetically defined glycosylated mannose-functionalized Aib-peptide as the second component display similar features, thereby providing reproducible substrates suitable for the controlled display of bioactive carbohydrate ligands. The efficiency of such Aib-based SAMs as a biomolecular recognition platform was evidenced by examining the mannose-concanavalin A interaction via surface plasmon resonance biosensing. (literal)
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