6 research outputs found
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 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
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 \u3b1-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