Earticle

초록

영어

Elastin-like polypeptides (ELPs) are a family of polypeptides derived from a pentapeptide Val-Pro-Gly-Xaa-Gly repeat in the amino acid sequence of mammalian elastin. ELPs undergo a thermodynamically driven phase transition, characterized by intramolecular coacervation at
the inverse transition temperature (Tt). Because of their specific thermal behavior, ELPs have been applied to the various fields including protein purification (ITC), biosensors for heavy metals removal, and drug carrier scaffolds. Despite the extensive application and valuable usefulness of these materials, it has some challenges to synthesize the long ELPs in
vivo. First of all, repetitive units in ELPs gene are easily eliminated in the E.coli cells. In addition, owing to slipped strand mispairing, insufficiency of tRNA for translation, causative mutation in the translation process can occur frequently. Thus the productivity of the long ELPs are much lower
than those of the short ELPs in the same condition. To break through these shortcomings, we used cell-free protein synthesis system. By selective addition of specific amino acids constituting ELPs, we improved the productivity of the long ELPs. It is thought that this technique can be more effective in producing longer repetitive polypeptides or in preventing mutation caused by the insufficiency of specific amino acids.

키워드

저자

• Hun Su CHU [ School of Chemical and Biological Engineering, Seoul National University, Gwanak-gu, Seoul 151-742, Korea ]
• Jong In WON [ Department of Chemical Engineering, Hongik University, Mapo-gu, Seoul 121-791, Korea. ]

참고문헌

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간행물

표지보기 관심저널 등록

• 간행물명

  한국생물공학회 학술대회

• 간기

  반년간

• 수록기간

  1985~2013

• 십진분류

  KDC 476 DDC 576