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Development of Artificial Chaperone using Poly-γ-Glutamic Acid-Cholesterol Nanoparticle

등록일
2009년 8월 21일 15시 23분 30초
접수번호
1527
발표코드
36P200포 이곳을 클릭하시면 발표코드에 대한 설명을 보실 수 있습니다.
발표시간
목 <발표Ⅱ>
발표형식
포스터
발표분야
생명화학
저자 및
공동저자
곽미선, 홍승표1, 정동진1, 함수정, 임용택2, 김철중2, 성문희
국민대학교, Korea
1(주)바이오리더스, Korea
2충남대학교, Korea
An artificial chaperone, which can decrease the protein aggregation and increase the activation yield of denatured protein, was developed using poly-γ-glutamic acid-cholesterol conjugate(γ-PGA-cholesterol conjugate). γ-PGA-cholesterol conjugate is composed of hydrophilic γ-PGA backbone and partly substituted hydrophobic cholesterol, and is capable of forming a nanoparticle by the self-association in water. The γ-PGA-cholesterol nanoparticle have the ability to trap and release protein by host-guest interaction of the cholesterol group and β-cyclodextrin, suggested the molecular chaperone activity for refolding of denatured protein. We studied the artificial chaperone activity of γ-PGA-cholesterol nanoparticle by refolding of M2-HA (W150) fusion protein. HA (hemagglutinin) and M2 (matrix protein 2) are the protein that exist on the surface of AI (avian influenza) virus. M2-HA (W150) fusion protein was over-expressed as an insoluble form in E. coli. The insoluble M2-HA (W150) fusion protein was refolded by γ-PGA-cholesterol nanoparticle. The renaturation yield of insoluble M2-HA (W150) fusion protein reached approximately 35%. It is considered that the γ-PGA-cholesterol nanoparticle can be used as an artificial chaperone and can be applied for protein refolding. [This work was supported by Top Brand Project grant from Korea Research Council of Fundamental Science & Technology and KRIBB Initiative program (KGM3110912).]

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