In trifluoroethanol, oxytocin bound Ca2+ (Kd approximately 50 microM), causing CD and fluorescence changes that led to a helical conformation.
In plain wordsIn lab tests, calcium bound to oxytocin and shifted it toward a helical shape.
- Peptide
- Oxytocin
- Outcome
- Not applicableCa2+ binding and conformation of oxytocin
- Study
n: not reported in source
trifluoroethanol, CD and fluorescence spectroscopy- Outcome group
- Receptor activity and mechanism · Pharmacology
Measurements
- Kd
- ≈ 50 µM
- Ca2+ binding to oxytocin in trifluoroethanol
Source sentences
Binding Ca2+ (Kd approximately 50 microM) caused drastic CD and fluorescence changes leading to a helical conformation.
1 context sentence(design, population, supporting numbers)
To characterize the cation-bound form of oxytocin, we monitored the binding of Ca2+ and Mg2+ to oxytocin as well as peptides representing its ring and tail regions in trifluoroethanol, a lipid-mimetic solvent, using CD and fluorescence spectroscopy.
In this study, Oxytocin was a lab tool or a carrier, part of a mix, or the subject of a lab method. This result is not evidence about taking Oxytocin.