期刊
ACS CHEMICAL NEUROSCIENCE
卷 1, 期 7, 页码 495-504出版社
AMER CHEMICAL SOC
DOI: 10.1021/cn1000205
关键词
5-Hydroxytryptamine; membrane-associated receptors; receptor binding; functionalized surfaces; self-assembled monolayers; chemical patterning
资金
- Pennsylvania State University Center for Nanoscale Science
- National Science Foundation Materials Research and Science Engineering Center [DMR-0820404]
- LAM Research Corporation
- Kavli Foundation
Recognition of small diffusible molecules by large biomolecules is ubiquitous in biology. To investigate these interactions, it is important to be able to immobilize small ligands on substrates; however, preserving recognition by biomolecule-binding partners under these circumstances is challenging. We have developed methods to modify substrates with serotonin, a small-molecule neurotransmitter important in brain function and psychiatric disorders. To mimic soluble serotonin, we attached its amino acid precursor, 5-hydroxytryptophan, via the ancillary carboxyl group to oligo(ethylene glycol)terminated alkanethiols self-assembled on gold. Anti-5-hydroxytryptophan antibodies recognize these substrates, demonstrating bioavailability. Interestingly, 5-hydroxytryptophan-functionalized surfaces capture membrane-associated serotonin receptors enantio-specifically. By contrast, surfaces functionalized with serotonin itself fail to bind serotonin receptors. We infer that recognition by biomolecules evolved to distinguish small-molecule ligands in solution requires tethering of the latter via ectopic moieties. Membrane proteins, which are notoriously difficult to isolate, or other binding partners can be captured for identification, mapping, expression, and other purposes using this generalizable approach.
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