Identification and Characterization of Peptides Binding AgEG1 from a Phage Display Library

• 出 处: Forestry Studies in China
• 发表日期: 2005年04期
• 关键词: Phage phage library screening Coleoptera nylon chemically digestion sequencing s

Endoglucanases are the main cellulolytic enzymes of Anoplophora glabripennis. Their high activities in cellulose digestion as well as its good kinetic properties make it an attractive target for development of cellulase inhibitors. In this study, ran- dom peptide phage display technology was employed to identify peptides that bound the AgEG1, a member of endoglucanase isozymes. Phage clones with peptide LPPNPTK and XPP (X is residue T, L, A or H) motif frequently occurred in the selected phage population and showed a higher phage recovery than other clones. Peptide LPPNPTK was chemically synthesized and characterized for its binding activities to AgEG1. The synthetic peptide exhibited high specificity for AgEG1. The peptide LPPNPTK has the po- tential to be developed into inhibitors of the endoglucanase of A. glabripennis.

Endoglucanases are the main cellulolytic enzymes of Anoplophora glabripennis. Their high activities in cellulose digestion as well as its good kinetic properties make it an attractive target for the development of cellulase inhibitors. In this study, ran- dom peptide phage display technology was employed to identify peptides that bound the AgEG1, a member of endoglucanase isozymes. Phage clones with peptide LPPNPTK and XPP (X is residue T, L, A or H) motif 3 in the selected phage population and showed a higher phage recovery than other clones. Peptide LPPNPTK was chemically synthesized and characterized for its binding activities to AgEG1. The synthetic peptide exhibition high specificity for AgEG1. The peptide LPPNPTK has the po- tential to be developed into inhibitors of the endoglucanase of A. glabripennis.