Abstract
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.
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Acknowledgements
We thank Prof. Takahiro Sato at Osaka University for the fruitful discussion and Dr. Noboru Ohta (SPring-8), Prof. Noriyuki Igarashi (KEK), and Prof. Nobutaka Shimizu (KEK) for the SAXS measurements. The SAXS data were acquired at the BL40B2 beamline in SPring-8 with the approval of the Japan Synchrotron Radiation Research Institute (JASRI) (Proposal Nos. 2015B1100, 2016A1053, and 2016B1088) and at the BL-10C beamline in KEK-PF under the approval of the Photon Factory Program Advisory Committee (Proposal No. 2011G557). This work was partially supported by JSPS KAKENHI Grant Nos. JP17K05884 and JP18H02020.
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Ishida, S., Yoshida, T. & Terao, K. Complex formation of a triple-helical peptide with sodium heparin. Polym J 51, 1181–1187 (2019). https://doi.org/10.1038/s41428-019-0234-z
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DOI: https://doi.org/10.1038/s41428-019-0234-z
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