지원사업
학술연구/단체지원/교육 등 연구자 활동을 지속하도록 DBpia가 지원하고 있어요.
커뮤니티
연구자들이 자신의 연구와 전문성을 널리 알리고, 새로운 협력의 기회를 만들 수 있는 네트워킹 공간이에요.
초록· 키워드
오류제보하기
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 -4.5 kcal 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.
목차
Abstract
1. Introduction
2. Experiment
3. Results and Discussion
4. Conclusions
References
참고문헌 (23)
참고문헌 신청
J. Seelig and P. Ganz, Biochemistry, 30(38), 9354-9 (1991).
A. Seelig and P. M. Macdonald, Biochemistry, 28(6), 2490-6 (1989).
T. L. Whitehead, L. M. Jones, and R. P. Hicks, Journal of Biomolecular Structure and Dynamics, 21(4), 567- 576 (2004).
P. Ram and J. H. Prestegard, BBA - Biomembranes, 940(2), 289-294 (1988).
T. L. Whitehead, L. M. Jones, and R. P. Hicks, Biopolymers, 58(7), 593-605 (2001).
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