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Selecting and Identification of Binding Peptides of the Endoglucanases from Anoplophora glabripennis

  • Received Date: 2006-01-10
  • Endoglucanases are the main cellulolytic enzymes in the gut of Anoplophora glabripennis.In this study,random peptide phage display technology was employed to screen peptides that bound the AgEG2,a member of endoglucanase isozymes.Phage clones displaying peptide TPHRSPL accounted for 33.7% of the selected phage population after three rounds of screening,and showed higher phage recovery than the other clones in the binding assay.Peptide TPHRSPL was chemically synthesized and tested for its binding activity to AgEG2.The synthetic peptide exhibited high binding specificity for AgEG1 and AgEG2.This indicated that peptide TPHRSPL had the affinity to the endoglucanase of A.glabripenni,which could be used to study the biological role of the enzyme in the gut,and had the potential to be developed into biological control agents of A.glabripenni.
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Selecting and Identification of Binding Peptides of the Endoglucanases from Anoplophora glabripennis

  • 1. Key Laboratory for Silviculture and Conservation of Ministry of Education, Beijing Forestry University, Beijing 100083, China
  • 2.  Research Institute of Forestry, CAF, Key Laboratory of Tree Breeding and Cultivation, State Forestry Administration, Beijing 100091, China
  • 3. Research Institute of Forestry, CAF, Key Laboratory of Tree Breeding and Cultivation, State Forestry Administration, Beijing 100091, China
  • 4. Key Laboratory of Genetics and Breeding in Trees and Ornamental Plant, Ministry of Education, Beijing Forestry University, Beijing 100083, China

Abstract: Endoglucanases are the main cellulolytic enzymes in the gut of Anoplophora glabripennis.In this study,random peptide phage display technology was employed to screen peptides that bound the AgEG2,a member of endoglucanase isozymes.Phage clones displaying peptide TPHRSPL accounted for 33.7% of the selected phage population after three rounds of screening,and showed higher phage recovery than the other clones in the binding assay.Peptide TPHRSPL was chemically synthesized and tested for its binding activity to AgEG2.The synthetic peptide exhibited high binding specificity for AgEG1 and AgEG2.This indicated that peptide TPHRSPL had the affinity to the endoglucanase of A.glabripenni,which could be used to study the biological role of the enzyme in the gut,and had the potential to be developed into biological control agents of A.glabripenni.

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