学術雑誌論文

学術雑誌論文

text

Polymer Journal. 2019, 51(11), p. 1181-1187

Complex formation of a triple-helical peptide with sodium heparin

Nature Publishing Group

英語

text

2019-11

https://doi.org/10.1038/s41428-019-0234-z

Ishida, S., Yoshida, T. & Terao, K. (2019) "Complex formation of a triple-helical peptide with sodium heparin," Polymer Journal, 51, 11, pp. 1181–1187.

Small-angle X-ray scattering (SAXS) and circular dichroism measurements were carried out for NaHeparin and a triple-helical peptide, H-(Pro-Pro-Gly)10-OH (PPG10), in aqueous sodium chloride (NaCl) at ionic strengths of 20, 50, and 150 mM at different temperatures. While PPG10 forms a triple helix below 25 °C, the melting temperature of the triple helix in the mixed solution is considerably higher (~10 °C) at low CS values than without NaHeparin. Part of the PPG10 molecules formed complexes with NaHeparin in 20 and 50 mM aqueous NaCl at 15 °C, but all solutes were molecularly dispersed at 75 °C, indicating that only triple helices form complexes with NaHeparin. Electrostatic attraction plays an important role in the complexation, since no complex formation was observed in 150 mM aqueous NaCl. The scattering function of the complex was explained by the presence of a thick wormlike chain, indicating that the molecular shape is different from that of the previously investigated complex with polyacrylic acid and carboxymethyl amylose. This suggests appreciable attractive interaction between the triple-helical part of PPG10 and NaHeparin.

77641

Complex formation of a triple-helical peptide with sodium heparin

Nature Publishing Group

英語

2019-11

Polymer Journal

51

11

1181

1187

https://doi.org/10.1038/s41428-019-0234-z

https://hdl.handle.net/11094/77641