Conformationally constrained functional peptide monolayers for the controlled display of bioactive carbohydrate ligands

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 we...

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Veröffentlicht in:Langmuir : the ACS journal of surfaces and colloids. - 1992. - 29(2013), 26 vom: 02. Juli, Seite 8187-92
1. Verfasser: Kaplan, Justin M (VerfasserIn)
Weitere Verfasser: Shang, Jing, Gobbo, Pierangelo, Antonello, Sabrina, Armelao, Lidia, Chatare, Vijay, Ratner, Daniel M, Andrade, Rodrigo B, Maran, Flavio
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2013
Zugriff auf das übergeordnete Werk:Langmuir : the ACS journal of surfaces and colloids
Schlagworte:Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Aminoisobutyric Acids Immobilized Proteins Peptides Sulfhydryl Compounds Concanavalin A 11028-71-0 mehr... 2-aminoisobutyric acid 1E7ZW41IQU Gold 7440-57-5 Mannose PHA4727WTP
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245 1 0 |a Conformationally constrained functional peptide monolayers for the controlled display of bioactive carbohydrate ligands 
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520 |a 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 
650 4 |a Journal Article 
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650 4 |a Research Support, Non-U.S. Gov't 
650 4 |a Research Support, U.S. Gov't, Non-P.H.S. 
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650 7 |a 7440-57-5  |2 NLM 
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700 1 |a Shang, Jing  |e verfasserin  |4 aut 
700 1 |a Gobbo, Pierangelo  |e verfasserin  |4 aut 
700 1 |a Antonello, Sabrina  |e verfasserin  |4 aut 
700 1 |a Armelao, Lidia  |e verfasserin  |4 aut 
700 1 |a Chatare, Vijay  |e verfasserin  |4 aut 
700 1 |a Ratner, Daniel M  |e verfasserin  |4 aut 
700 1 |a Andrade, Rodrigo B  |e verfasserin  |4 aut 
700 1 |a Maran, Flavio  |e verfasserin  |4 aut 
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