Samples of P26 (0.2 mg/ mL), Type I collagen (1 mg/mL) and P26-collagen mix were dissolved in HEPES buffer (10mM) t pH 7.15 and incubated for 30 min at RT. Circular Dichroism (CD) spectra were collected in high-transparency quartz cuvettes (250 μL) with a path length of 1 mm and band width of 2 nm at 25 °C in the far UV spectral range (190–260 nm) using a JASCO J-815 circular dichroic spectrometer. Conformational changes in the secondary structure of the peptide induced by collagen were investigated at physiological pH by subtracting the spectra of collagen alone.45 (link) All the CD spectra collected were normalized to mean residual ellipticity (MRE) values.
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Circular Dichroism Analysis of P26-Collagen Interactions
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Corresponding Organization : University of Southern California
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Variable analysis
independent variables
- Concentration of P26 (0.2 mg/mL)
- Concentration of Type I collagen (1 mg/mL)
- P26-collagen mix
- Conformational changes in the secondary structure of the peptide induced by collagen
- Circular Dichroism (CD) spectra collected in the far UV spectral range (190–260 nm)
- HEPES buffer (10mM) at pH 7.15
- Incubation time of 30 min at room temperature (RT)
- Measurement conditions: high-transparency quartz cuvettes (250 μL), path length of 1 mm, band width of 2 nm, temperature of 25 °C
- Collagen alone (negative control)
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