Interaction of human parathyroid hormone fragment 1-34 (hPTH 1–34) with dodecylphosphocholine (DPC) micelle has been investigated by UV/Vis, fluorescence, circular dichroism (CD), and NMR spectroscopy. The interaction was noted by the bathochromic shift and hyperchromic shift in UV/Vis spectra. In fluorescence study, both the intensity-enhancing effect and a blue shift are observed for the maximum wavelength in the emission spectra. Pulse magnetic field gradient NMR experiment found that the binding constant (Kα) of hPTH (1-34) with DPC micelles were 5.84 ×103 M-1, and the free energy (ΔG0) was -21.5 kJ/mol, which indicates a spontaneous interaction between hPTH (1-34) and DPC micelles. The CD spectra showed that introducing the DPC micelle into the peptide aqueous solution increased the α-helix structure from 0-40%, while the β-sheet decreased from 78-45%.

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