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Selective lead adsorption by recombinant Escherichia coli displaying a lead-binding peptide.
Nguyen, Thuong T L,Lee, Hae Ryong,Hong, Soon Ho,Jang, Ji-Ryang,Choe, Woo-Seok,Yoo, Ik-Keun Humana Press 2013 Applied biochemistry and biotechnology Vol.169 No.4
<P>A highly specific lead-binding peptide ThrAsnThrLeuSerAsnAsn was displayed on Escherichia coli, and lead adsorption characteristics of the recombinant bacteria were investigated. Cell surface-displayed peptide was expressed under the control of an arabinose promoter using outer membrane protein C (OmpC(t)) as an anchoring motif. The optimal induction period and arabinose concentration for the expression of peptide-fused OmpC(t) were determined to be 2?h and 0.001?g/L, respectively. Selective adsorption of Pb(2+) onto recombinant cells was verified with individual or combinatory use of four metal ions, Pb(2+), Ni(2+), Co(2+), and Cu(2+); the amount of bound Pb(2+) onto the biosorbents was significantly higher than the other metal ions. The adsorption isotherm of recombinant cells for Pb(2+) followed the Langmuir isotherm with a maximum adsorption loading (q (max)) of 526?μmol/g dry cell weight.</P>
바이오패닝에 의한 Pb2+ 친화성 펩타이드 서열의 탐색
Thuong T. L. Nguyen,홍순호,최우석,유익근 한국생물공학회 2013 KSBB Journal Vol.28 No.3
For the selection of peptide specifically binding to Pb²+, the biopanning with the commercially available Ph.D.-7phage displayed heptapeptide library was carried out against Pb²+ immobilized on a metal-chelating IDA (iminodiaceticacid) resin. After four rounds of screening against Pb²+-IDA including negative selections against charged bead with metalions other than Pb²+ and uncharged bead, several candidate leadbindingphage peptides were initially determined based on theorder of frequency from the screened phage clones. Of theselected phage peptide sequences, the peptide of the highestfrequency, CysSerIleArgThrLeuHisGlnCys (CSIRTLHQC)also exhibited the strongest affinity for Pb²+ in binding assaysfor individual phage clones. However, there was not a significantdifference in Pb²+ affinity between selected peptides whenusing synthetic heptapeptides corresponding to the displayedpeptide sequences of phage clones.
바이오패닝에 의한 Pb<SUP>2+</SUP> 친화성 펩타이드 서열의 탐색
Thuong T. L. Nguyen,홍순호(Soon Ho Hong),최우석(Woo-Seok Choe),유익근(Ik-Keun Yoo) 한국생물공학회 2013 KSBB Journal Vol.28 No.3
For the selection of peptide specifically binding to Pb2+, the biopanning with the commercially available Ph.D.-7 phage displayed heptapeptide library was carried out against Pb2+ immobilized on a metal-chelating IDA (iminodiacetic acid) resin. After four rounds of screening against Pb<SUP>2+</SUP>-IDA including negative selections against charged bead with metal ions other than Pb2+ and uncharged bead, several candidate leadbinding phage peptides were initially determined based on the order of frequency from the screened phage clones. Of the selected phage peptide sequences, the peptide of the highest frequency, CysSerIleArgThrLeuHisGlnCys (CSIRTLHQC) also exhibited the strongest affinity for Pb<SUP>2+</SUP> in binding assays for individual phage clones. However, there was not a significant difference in Pb2+ affinity between selected peptides when using synthetic heptapeptides corresponding to the displayed peptide sequences of phage clones.