DOI QR코드

DOI QR Code

Thermodynamics of the binding of Substance P to lipid membranes

  • Lee, Woong Hyoung ;
  • Kim, Chul
  • Received : 2017.01.22
  • Accepted : 2017.03.01
  • Published : 2017.04.25

Abstract

The thermodynamic functions for the binding of the peptide Substance P (SP) on the surface of lipid vesicles made of various types of lipids were obtained by using isothermal titration calorimetry. The reaction enthalpies measured from the experiments were -0.11 to $-4.5kcal\;mol^{-1}$. The sizes of the lipid vesicles were measured with dynamic light scattering instrument in order to get the correlation between the reaction enthalpies and the vesicle sizes. The bindings of SP on the lipid vesicles with diameter of 37 to 108 nm were classified into the enthalpy-driven reaction or the entropy-driven reaction according to the size of the lipid vesicles. For the enthalpy-driven binding reaction, the significance of the electrostatic interactions between SP and lipid molecules was affirmed from the experimental results of the DMPC/DMPG/DMPH and DMPC/DMPS/DMPH vesicles as well as the importance of the hydrophobic interactions between hydrophobic groups of SP and lipid molecules.

Keywords

thermodynamics;partitioning;Substance P;lipid vesicle

References

  1. J. Seelig and P. Ganz, Biochemistry, 30(38), 9354-9 (1991). https://doi.org/10.1021/bi00102a031
  2. A. Seelig and P. M. Macdonald, Biochemistry, 28(6), 2490-6 (1989). https://doi.org/10.1021/bi00432a021
  3. T. L. Whitehead, L. M. Jones, and R. P. Hicks, Journal of Biomolecular Structure and Dynamics, 21(4), 567-576 (2004). https://doi.org/10.1080/07391102.2004.10506949
  4. P. Ram and J. H. Prestegard, BBA - Biomembranes, 940(2), 289-294 (1988). https://doi.org/10.1016/0005-2736(88)90203-9
  5. T. L. Whitehead, L. M. Jones, and R. P. Hicks, Biopolymers, 58(7), 593-605 (2001). https://doi.org/10.1002/1097-0282(200106)58:7<593::AID-BIP1033>3.0.CO;2-P
  6. G. Beschiaschvili and J. Seelig, Biochemistry, 31(41), 10044-10053 (1992). https://doi.org/10.1021/bi00156a026
  7. T. C. Wong and X. Gao, Biopolymers, 45(5), 395-403 (1998). https://doi.org/10.1002/(SICI)1097-0282(19980415)45:5<395::AID-BIP7>3.0.CO;2-G
  8. D. A. Keire and T. G. Fletcher, Biophysical J., 70(4), 1716-1727 (1996). https://doi.org/10.1016/S0006-3495(96)79734-5
  9. S. Auge, B. Bersch, M. Tropis, and A. Milon, Biopolymers, 54(5), 297-306 (2000). https://doi.org/10.1002/1097-0282(20001015)54:5<297::AID-BIP10>3.0.CO;2-9
  10. T. Wieprecht, M. Beyermann, and J. Seelig, Biophys Chem, 96(2-3), 191-201 (2002). https://doi.org/10.1016/S0301-4622(02)00025-X
  11. C. Kim, S. B. Baek, D. H. Kim, S. C. Lim, H. J. Lee, and H. C. Lee, J. Peptide Sci., 15(5), 353-358 (2009). https://doi.org/10.1002/psc.1121
  12. B. Barz, T. C. Wong, and I. Kosztin, Biochim Biophys Acta, 1778(4), 945-53 (2008). https://doi.org/10.1016/j.bbamem.2007.11.014
  13. S. Harrison and P. Geppetti, Int. J. Biochem Cell. Biol., 33(6), 555-76 (2001). https://doi.org/10.1016/S1357-2725(01)00031-0
  14. T. Hokfelt, B. Pernow, and J. Wahren, J Intern Med, 249(1), 27-40 (2001).
  15. H. Duplaa, O. Convert, A. M. Sautereau, J. F. Tocanne, and G. Chassaing, Biochimica et Biophysica Acta - Biomembranes, 1107(1), 12-22 (1992). https://doi.org/10.1016/0005-2736(92)90323-E
  16. A. Seelig, T. Alt, S. Lotz, and G. Holzemann, Biochemistry, 35(14), 4365-74 (1996). https://doi.org/10.1021/bi952434q
  17. I. Jelesarov and H. R. Bosshard, J. Mol. Recognit, 12(1), 3-18 (1999). https://doi.org/10.1002/(SICI)1099-1352(199901/02)12:1<3::AID-JMR441>3.0.CO;2-6
  18. N. Voievoda, T. Schulthess, B. Bechinger, and J. Seelig, J Phys Chem B, 119(30), 9678-87 (2015). https://doi.org/10.1021/acs.jpcb.5b04543
  19. M. N. Triba, D. E. Warschawski, and P. F. Devaux, Biophys J, 88(3), 1887-901 (2005). https://doi.org/10.1529/biophysj.104.055061
  20. J. Seelig, Biochim Biophys Acta, 1666(1-2), 40-50 (2004). https://doi.org/10.1016/j.bbamem.2004.08.004
  21. T. Broemstrup and N. Reuter, Biophysical J., 99, 825- 833 (2010). https://doi.org/10.1016/j.bpj.2010.04.064
  22. T. Wymore and T. C. Wong, Biophysical J., 76, 1213-1227 (1999). https://doi.org/10.1016/S0006-3495(99)77285-1
  23. M. Meier and J. Seelig, J. Mol. Biol., 369(1), 277-89 (2007). https://doi.org/10.1016/j.jmb.2007.02.082

Acknowledgement

Supported by : Hannam University