abs

학술발표회초록보기

초록문의 abstract@kcsnet.or.kr

결제문의 member@kcsnet.or.kr

현재 가능한 작업은 아래와 같습니다.
  • 09월 04일 17시 이후 : 초록수정 불가능, 일정확인 및 검색만 가능

제114회 대한화학회 학술발표회, 총회 및 기기전시회 안내 Expression, Purification and NMR Structural Studies of syndecan-4 as a cell surface receptor

등록일
2014년 8월 28일 17시 23분 33초
접수번호
1358
발표코드
PHYS.P-471 이곳을 클릭하시면 발표코드에 대한 설명을 보실 수 있습니다.
발표시간
10월 15일 (수요일) 16:00~19:00
발표형식
포스터
발표분야
물리화학
저자 및
공동저자
한선필, 김태형, 김지선, 최성섭, 김용애*
한국외국어대학교 화학과, Korea
Syndecans as cell surface receptors participate in biologically important cell-cell and cell-matrix interactions. They have a common basic structure including modified extracellular domains, conserved transmembrane and cytoplasmic domains. One of them, syndecan-4 may affect tissue development and repair as well as the pathogenesis of numerous diseases, especially such as cancer. The transmembrane domain of syndecan-4(Syd4) consists of 25 hydrophobic amino acids. It performs the formation of dimer or oligomer and is crucial for transduction of signals. Even though, a lot of efforts to elucidate the structure and function of them, it has been hindered by insufficient yields and low solubility. Thus, we demonstrated an optimized method for recombinant expression and purification of three kinds of Syd4 like wild type Syd4-TM(wt-Syd4), mutant Syd4-TM(mSyd4), and Syd4-eTC. The mSyd4 has a partially modified sequence of wt-Syd4 and the Syd4-eTC has extracellular, transmembrane and cytoplasmic domain of syndecan-4. All peptides were released from the fusion protein, and then purified by semi-preparative reversed-phase HPLC. Enough amounts of purified Syd4 series for the analysis of peptides was obtained from 1L of M9 minimal media under optimal conditions. Their biophysical properties of peptides were studied by CD, MS and NMR spectroscopy. Analysis of CD spectra presents that all types of Syd4 series adopt a stable α-helical structure in micelle environments. The solution NMR studies show wSyd4 and Syd4-eTC form an asymmetric dimer in micelles and mSyd4 present monomer. Optimized 3D structure and absolute tilt angle on membrane bilayers of Syd4 based on 2D SAMPI4 solid-state NMR and Molecular Dynamics Simulation are underway.

상단으로