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Serotonin, a crucial neurotransmitter synthesized by enterochromaffin cells, plays a cardinal role in regulating gastrointestinal (GI) motility. With over 90% of the body's total serotonin in the GI tract, its influence on digestive processes is profound. Serotonin is swiftly released upon various stimuli, such as food boluses or certain drugs, triggering intrinsic sensory neurons in the myenteric plexus and extrinsic vagal and spinal sensory neurons. This leads to the activation of the...
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Related Experiment Video

Updated: May 20, 2026

Thermostabilization, Expression, Purification, and Crystallization of the Human Serotonin Transporter Bound to S-citalopram
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Thermostabilization, Expression, Purification, and Crystallization of the Human Serotonin Transporter Bound to S-citalopram

Published on: November 27, 2016

Native serotonin membrane receptors recognize 5-hydroxytryptophan-functionalized substrates: enabling small-molecule

Amit Vaish1, Mitchell J Shuster, Sarawut Cheunkar

  • 1Department of Bioengineering Huck Institutes of the Life Sciences, Pennsylvania State University, University Park, Pennsylvania 16802, USA.

ACS Chemical Neuroscience
|July 11, 2012
PubMed
Summary

Researchers developed a novel method to immobilize serotonin for studying its interactions with biomolecules. This technique successfully captures serotonin receptors, offering new ways to study membrane proteins.

Keywords:
5-Hydroxytryptaminechemical patterningfunctionalized surfacesmembrane-associated receptorsreceptor bindingself-assembled monolayers

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Rapid In Situ Hybridization using Oligonucleotide Probes on Paraformaldehyde-prefixed Brain of Rats with Serotonin Syndrome

Published on: September 23, 2015

Area of Science:

  • Biochemistry
  • Neuroscience
  • Materials Science

Background:

  • Studying interactions between small molecules and large biomolecules is crucial in biology.
  • Immobilizing small ligands on surfaces while maintaining biomolecular recognition is challenging.
  • Serotonin, a neurotransmitter, plays a key role in brain function and psychiatric disorders.

Purpose of the Study:

  • To develop a method for immobilizing serotonin on substrates to study its interactions with binding partners.
  • To investigate whether immobilized serotonin can be recognized by biomolecules, particularly serotonin receptors.
  • To establish a generalizable approach for capturing and studying membrane proteins and other binding partners.

Main Methods:

  • Functionalization of gold substrates with oligo(ethylene glycol)-terminated alkanethiols.
  • Attachment of 5-hydroxytryptophan (serotonin precursor) to the functionalized substrates via its carboxyl group.
  • Testing the recognition of these surfaces by anti-5-hydroxytryptophan antibodies and serotonin receptors.
  • Comparison with surfaces functionalized directly with serotonin.

Main Results:

  • Successfully created surfaces functionalized with 5-hydroxytryptophan that were recognized by antibodies, confirming bioavailability.
  • Demonstrated that 5-hydroxytryptophan-functionalized surfaces capture membrane-associated serotonin receptors with enantioselectivity.
  • Observed that surfaces directly functionalized with serotonin failed to bind serotonin receptors.
  • Inferred that tethering small molecules via ectopic moieties is essential for biomolecular recognition.

Conclusions:

  • Biomolecular recognition of small molecules in solution requires specific tethering strategies, such as using ectopic moieties.
  • The developed method enables the capture and study of notoriously difficult-to-isolate membrane proteins.
  • This generalizable approach has significant implications for identifying, mapping, and expressing various binding partners.