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Identification of a Deoxyribonuclease I Inhibitor from a Phage-Peptide Library
최석정,Jeffery J. Sperinde,Francis C. Szoka Jr. 한국분자세포생물학회 2005 Molecules and cells Vol.19 No.1
Deoxyribonuclease I (DNase I) is a divalent cation de-pendent endonuclease and thought to be a significant barrier to effective gene delivery. The only known DNase I-specific inhibitor is monomeric actin which acts by forming a 1:1 complex with DNase I. Its use, however, is restricted because of tendency to polymer-ize under certain conditions. We screened two random phage peptide libraries of complexity 108 and 109 for DNase I binders as candidates for DNase I inhibitors. A number of DNase I-binding peptide sequences were identified. When these peptides were expressed as fu-sion proteins with Escherichia coli maltose binding protein, they inhibited the actin-DNase I interaction (IC50 = 0.10.7 M) and DNA degradation by DNase I (IC50 = 0.88 M). Plasmid protection activity in the presence of DNase I was also observed with the fusion proteins. These peptides have the potential to be a use-ful adjuvant for gene therapy using naked DNA