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Updated: Apr 28, 2026
Microfabrication of Nanoporous Gold Patterns for Cell-material Interaction Studies
Published on: July 15, 2013
Lectin-carbohydrate interactions on nanoporous gold monoliths
Yih Horng Tan1, Kohki Fujikawa2, Papapida Pornsuriyasak2
1Department of Chemistry and Biochemistry, University of Missouri - Saint Louis, Saint Louis, MO 63121, USA ; UM-St. Louis Center for Nanoscience, University of Missouri - Saint Louis, Saint Louis, MO 63121, USA.
Nanoporous gold (np-Au) surfaces modified with mannose-presenting self-assembled monolayers (SAMs) selectively capture Concanavalin A (Con A) lectin. This specific binding allows for the capture and release of carbohydrate-binding proteins, showcasing potential in glycoscience applications.
Area of Science:
- Biomaterials Science
- Surface Chemistry
- Glycoscience
Background:
- Nanoporous gold (np-Au) offers a versatile platform for surface modification.
- Self-assembled monolayers (SAMs) are crucial for tailoring surface properties.
- Carbohydrate-based recognition is vital in biological systems.
Purpose of the Study:
- To functionalize np-Au monoliths with carbohydrate-presenting SAMs for protein capture.
- To investigate the specificity and efficiency of Concanavalin A (Con A) binding.
- To explore the potential of these modified surfaces in glycoscience and glycotechnology.
Main Methods:
- Modification of np-Au monoliths with various thiols: octadecanethiol, 8-mercaptooctyl α-D-mannopyranoside (αMan-C8-SH), and 8-mercapto-3,6-dioxaoctanol (HO-PEG2-SH).
- Preparation and characterization of mixed SAMs.
- Thermogravimetric analysis (TGA) to quantify SAM loading and protein binding.
- Atomic force microscopy (AFM) to confirm protein presence.
Main Results:
- np-Au modified with αMan-C8-SH SAMs demonstrated specific binding of Con A.
- Mixed SAMs with HO-PEG2-SH showed higher specificity compared to those with octanethiol.
- Minimal non-specific binding of Con A was observed on HO-PEG2-SH modified surfaces.
- The mannoside-presenting surfaces showed selectivity for Con A over IgG and PNA.
- Con A could be eluted from the modified np-Au using methyl α-D-mannopyranoside.
Conclusions:
- Carbohydrate-modified np-Au monoliths are effective for the selective capture and release of carbohydrate-binding proteins like Con A.
- The developed system holds significant promise for applications in glycoscience and glycotechnology.
- TGA is a valuable tool for assessing protein binding and surface modification efficiency.
