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  • 08월 28일 16시 이후 : 초록수정 불가능, 일정확인 및 검색만 가능

Syndecan-4V cytoplasm fragment has selectivity to the membrane compositions

2008년 8월 11일 14시 48분 27초
33P188포 이곳을 클릭하시면 발표코드에 대한 설명을 보실 수 있습니다.
목 <발표Ⅰ>
저자 및
김시원, 이상미, 김석만
부산대학교 화학과, Korea
The Syndecans, a gene family of four transmembrane protecoglycans are the major source of the heparin sulfate. Syndecan-4 can regulate cell-matrix interactions and is enriched in focal adhesions. Recent studies have demonstrate that the cytoplasmic tail of syndecan-4 can activate protein kinase Cα in vitro, in combination with phosphatidylinsitol-4,5-bisphosphate (PIP2). The NMR structure of the Syndecan-4V was reported as a cramp like dimer-structure but the interactions with the membrane was not reported yet. We synthesized several different sequences of Syndecan-4V fragments using solid-phase synthetic method to investigate the aspects of the interactions between the Syndecan-4 cytoplasm regions and biological membrane. We prepared POPE, POPC single components and POPE/POPG and POPC/POPG binary components multilamellar vesicles (MLVs) to investigate the interactions between the peptides and membrane by the measuring of 31P solid-state NMR powder spectrum. Then chemical shift anisotropy (CSA) was calculated from the powder pattern spectrum to monitor the dynamic state of the phospholipid vesicles. The powder pattern spectrums were changed dramatically by the Syndecan-4V fragment and eventually, the crystalline state of the phospholipid bilayer was changed to small micelle like structure and the effects were severe in the PC and PG binary system. This result implying the Syndecan-4 fragment peptide might disrupt the mammalian cell membrane.