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Mutational Analysis of the Absolutely Conserved B8Gly: Consequence on foldability and Activity of Insulin

Acta Biochimica et Biophysica Sinica 2005年第10期37卷 673-679页

作者： Zhan-Yun GUO~1 Zhou ZHANG~1 Xiao-Yuan JIA~1 Yue-Hua TANG~(1,2) You-Min FENG~(1,2*) 1 Key Laboratory of Proteontics,Institute of Biochemistry,and Cell Biology,Shanghai Institutes for Biological Sciences.Chinese Academy of Sciences,Shanghai 200031.China 2 Instutute of Biochemistry,Zhejiang Sci-Tech University,Hangzhou 310018,China Key Laboratory of Proteomics Institute of Biochemistry and Cell Biology Shanghai Institutes for Biological Sciences Chinese Academy of SciencesShanghai 200031 China Institute of Biochemistry Zhejiang Sci-Tech UniversityHangzhou 310018 China

B8Gly is absolutely conserved in insulins during ***,its correspondingposition is always occupied by a Gly residue in other members of insulin *** work showedthat Ala replacement of BSGly significantly decreased both the activity and the foldability of *** effects of substitution are complicated,and different replacements sometimes cause significantly *** analyze the effects of B8 replacement by different amino acids,three new insulin/single-chaininsulin mutants with BSGly replaced by Ser,Thr or Leu were prepared by protein engineering,and both theirfoldability and activity were *** general,replacement of BSGly by other amino acids causes significantdetriment to the foldability of single-chain insulin:the conformations of the three B8 mutants are essentiallydifferent from that of wild-type molecules as revealed by circular dichroism;their disulfide stabilities inredox buffer are significantly decreased:their in vitro refolding efficiencies are decreased approximatelytwo folds;the structural stabilities of the mutants with Ser or Thr substitution are decreased significantly,while Leu substitution has little effect as measured by equilibrium guanidine *** far as biologicalactivity is *** replacement of B8Gly has only a moderate effect:its insulin receptor-bindingactivity is 23% of native *** Thr or Leu replacement produces significant detriment:the receptor-binding potencies of the two mutants are less than 0.2% of native *** present results suggest thatGly is likely the only applicable natural amino acid for the B8 position of insulin where both foldability andactivity are concerned.

关键词： insulin foldability activity disulfide stability

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