Conformationally constrained functional peptide monolayers for the controlled display of bioactive carbohydrate ligands.
Langmuir
; 29(26): 8187-92, 2013 Jul 02.
Article
em En
| MEDLINE
| ID: mdl-23782319
ABSTRACT
In this study, we employed thiolated peptides of the conformationally constrained, strongly helicogenic α-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.
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Base de dados:
MEDLINE
Assunto principal:
Peptídeos
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Compostos de Sulfidrila
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Proteínas Imobilizadas
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Ouro
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Ácidos Aminoisobutíricos
Idioma:
En
Ano de publicação:
2013
Tipo de documento:
Article