ArticleLangmuir : the ACS journal of surfaces and colloids2013
Conformationally constrained functional peptide monolayers for the controlled display of bioactive carbohydrate ligands.
Article in Langmuir : the ACS journal of surfaces and colloids, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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Who cites it
2 citing papers in PubMed.
- Reversible activation of pH-sensitive cell penetrating peptides attached to gold surfaces.Chemical communications (Cambridge, England) · 2015Article
- Are glycan biosensors an alternative to glycan microarrays?Analytical methods : advancing methods and applications · 2014Article
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Authors and funding
9 authors.
Funding
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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