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학술발표회초록보기

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제109회 대한화학회 학술발표회, 총회 및 기기전시회 안내 NMR Evidence of Motions in Heparin-Binding Domain of VEGF165 and Its complex with Inhibitor, Triamterene

등록일
2012년 2월 22일 19시 49분 40초
접수번호
1368
발표코드
PHYS.P-505 이곳을 클릭하시면 발표코드에 대한 설명을 보실 수 있습니다.
발표시간
4월 25일 (수요일) 18:00~21:00
발표형식
포스터
발표분야
물리화학
저자 및
공동저자
정기웅, 강동일1, 김양미
건국대학교 생명공학과, Korea
1건국대학교 화학과, Korea
It is known that vascular endothelial growth factor (VEGF) interacts with Ab by binding to heparin-binding domain (HBD) at C-terminal region of VEGF and is accumulated in the senile plaques of Alzheimer’s disease patients’ brains. In this study, we showed that triamterene (Trm) inhibits VEGF?Aβ interaction without affecting other biological activities of VEGF or Aβ. The results of binding study showed that the loop region (S11?L17) and F18 at the beginning of the first β-sheet in the HBD constitute the inhibitor binding site. Spin relaxation experiments and Model-free analysis showed that the residues in the disordered loop region of the N-terminus exhibited conformational exchanges in free HBD and these flexibility decreased dramatically upon binding to Trm. It suggests that Aβ as well as inhibitor may recognize these unique dynamic features of the HBD. Furthermore, C-terminal residues continued to exhibit slow conformational motions, even in the HBD?Trm complex, implying that these motions of the HBD might be important for interactions with heparin molecules. The flexibility of HBD should be essential for VEGF function and interaction with other protein partners.

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