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보고서 초록[개인신상정보 삭제]
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Contents 8
제1장 서론 13
가. 연구개발의 중요성 및 필요성 13
나. 연구개발의 국내외 현황 14
다. 연구개발대상 기술의 차별성 18
제2장 연구개발의 목표 및 내용 20
가. 연구의 최종목표 20
나. 연도별 연구개발의 목표 및 평가방법 20
다. 연도별 추진체계 21
제3장 연구개발 결과 및 활용계획 22
가. 연구개발 결과 및 토의 22
(1) Biopanning에 의한 Pb2+(이미지참조) 친화성 펩타이드 탐색 22
(2) 선별된 펩타이드의 Pb2+(이미지참조) 친화성 분석 26
(3) 펩타이드의 아미노산 서열 특이성 분석 31
(4) 특정 펩타이드를 함유한 개별 phage clone에 대한 Pb2+(이미지참조) 친화성 분석 33
(5) 선별된 펩타이드의 Pb2+(이미지참조) 선택 인지능 평가 36
(6) Chromatographic biopanning 기법을 이용한 Pb2+(이미지참조) 선택 친화성 펩타이드 탐색 39
(7) Chromatographic biopanning 기법에 의해 선별된 Pb2+(이미지참조) 친화성 펩타이드 분석 52
(8) 나노로드(nano-rod) 형태의 전도성 고분자 전극 제조 55
(9) 전도성고분자-IDA 기반 센서 개발 58
(10) 전도성고분자-펩타이드 기반 센서 개발 65
(11) Pb2+-친화성 펩타이드의 Pb2+ 인지능 및 다른 금속이온에 대한 교차인지능 평가(이미지참조) 71
나. 연구개발 결과 요약 74
(1) 전통적인 Biopanning 기법을 이용한 Pb2+(이미지참조) 친화성 펩타이드 탐색 74
(2) 신규 펩타이드 서열 탐색법인 Chromatographic Biopanning 기법 개발 및 활용 75
(3) 전도성 고분자-펩타이드 기반 Pb2+(이미지참조) 센서 모듈 개발 75
다. 연도별 연구개발목표의 달성도 77
라. 연도별 연구성과(논문/특허 등) 79
마. 관련분야의 기술발전 기여도 79
바. 연구개발 결과의 활용계획 80
제4장 참고문헌 81
Table 1.1. Examples of biosensors for different environmental applications. 16
Table 3.1: Summary of four rounds of biopanning for the screening Pb2+(이미지참조) binding phage particles. 25
Table 3.2: Selection of phage particles lacking cross binding affinity towards five different metal ions of positive charge valency of 2. 26
Table 3.3: Summary of chormatographic biopanning using imidazole gradient elution method. 28
Table 3.4: Summary of peptide seequences fractionated following the step gradient imidazole elution. 29
Table 3.5: Analysis of amino acid composition for 15 Pb2+(이미지참조)-binding peptides. 31
Table 3.6: Grouping of phage clones based on their relative binding stregnth to Pb2+(이미지참조). The grouping is based on the following criteria 35
Table 3.7: Summary of titering of phage particles in each round of chromatographic biopanning procedures. 45
Table 3.8: Analysis of Pb2+(이미지참조)-affinity peptide. 54
Figure 1.1. 환경오염물질 정량에 사용되는 기존 분석방법 및 바이오센서를 이용한 정량법 비교. 18
Figure 3.1: Schematics of Pb2+(이미지참조) binding peptide screening procedures. 23
Figure 3.2: Number of eluted phages in each round of the biopanning procedure. 25
Figure 3.3: Elution profiles of phage particles at varying imidazole concentrations. 28
Figure 3.4: Frequency of 15 Pb2+(이미지참조)-affinity peptides recruited from 10 imidazole elution fractions. 20 random samples were selected from each elution fraction to analyze the peptide sequence. 30
Figure 3.5: Amount of phage particles captured by Pb2+(이미지참조)-IDA resin for 15 phage clones. 34
Figure 3.6: Cross bindng of 15 selected peptide sequences to Ca2+(이미지참조). 37
FIgure 3.7: Cross bindng of 15 selected peptide sequences to Co2+, Cu2+, Ni2+, Zn2+.(이미지참조) 38
Figure 3.8: A schematic to show the feasibility of developing a new chromatographic library panning protocol 40
Figure 3.9: FPLC system used for chromatographic library panning developed in this study. 41
Figure 3.10: CIM monolithic column (Biaseparation, cat # 217.3010) used for immobilizing metal ions used during the chromatographic biopanning 41
Figure 3.11: Chromatographic biopanning procedure. 42
Figure 3.12: Confirmation of Pb2+(이미지참조) adsorption onto monolith column by UV monitoring (green line). 43
Figure 3.13: Effect of pH on the binding of Pb2+(이미지참조) to monolithic column. 44
Figure 3.14: Pre-negative biopanning: chromatographic monitoring of selecting phage particles lacking affinity to the resin per se m total recycling mode in order to efficiently remove any phage particles showing affiity to the resin by promoting the efficiency of multistage equilibrium adsorption. 44
Figure 3.15: The 1st round of chromatographic main biopanning. 46
Figure 3.16: The 2nd round of chromatographic main biopanning. 46
Figure 3.17: The 3rd round of chromatographic main biopanning. 47
Figure 3.18: The 1st round of chromatographic post-negative panning againt resin. 47
Figure 3.19: The 2nd round of chromatographic post-negative panning againt resin. 48
Figure 3.20: The 3rd round of chromatographic post-negative panning againt resin. 48
Figure 3.21: Elution profile of the 1st round post-negative selection against Cu2+(이미지참조). 49
Figure 3.22: Elution profile of the 2nd round post-negative selection against Cu2+(이미지참조). 49
Figure 3.23: Elution profile of the 3rd round post-negative selection against Cu2+(이미지참조). 50
Figure 3.24: Elution profile of the 1st round post-negative selection against Ni2+(이미지참조). 50
Figure 3.25: Elution profile of the 2nd round post-negative selection against Ni2+(이미지참조). 50
Figure 3.26: Elution profile of the 3rd round post-negative selection against Ni2+(이미지참조). 51
Figure 3.27: Elution profile of the 1st round post-negative selection against Co2+(이미지참조). 51
Figure 3.28: Elution profile of the 1st round post-negative selection against Co2+(이미지참조). 51
Figure 3.29: Elution profile of the 1st round post-negative selection against Fe3+(이미지참조). 52
Figure 3.30: Procedure used for the fabrication of the PPy/Au nanorod electrode using an AAO template 56
Figure 3.31: SEM images of Au plating for 1.0 C·cm-2(이미지참조) in AAO. 57
Figure 3.32: SEM- images 58
Figure 3.33: The relationship between the length of the PPy nanorods and applied charge. 58
Figure 3.34: A schematic of preparation of modified electrode and its putative interaction with metal ions. 59
Figure 3.35: SEM image of the 3MT/3TA copolymer film 60
Figure 3.36: SWV curves recorded at three different types of electrodes : 3MT/3TA copolymer (solid line), amine-modified(modfied) copolymer (dash line), IDA-modified copolymer (dash-dotline) electrode. 61
Figure 3.37: SWV curves recorded at the IDA-modified copolymer electrode immersed in 0.1 Macetate buffer solution containing 10μM Cu2+ and Pb2+, respectively.(이미지참조) 62
Figure 3.38: Stripping peak current for dissolution of metal ions captured by IDA-modified copolymer electrode following its immersion for varying time periods in acetate buffer solution supplemented with 10 μM of Cu2+ or Pb2+.(이미지참조) 62
Figure 3.39: Stripping peak current for dissolution of metal ions captured by IDA-modified copolymer electrode following its immersion in acetate buffer solutions supplemented with varying concentrations of Cu2+, Pb2+ and other metal ions.(이미지참조) 63
Figure 3.40: SWV curves and stripping peak current for dissolution of metal ions captured by IDA-modified copolymer electrode following its immersion in acetate buffer solutions supplemented with varying concentrations of Cu2+ in the presence of 20 μM Pb2+.(이미지참조) 63
Figure 3.41: SWV curves of the IDA-modified electrode: in 10μM Cu2+ solution (solid line); with EDTA-treatment (dash line); in 10μM Cu2+ solution after regeneration (dash-dot line).(이미지참조) 64
Figure 3.42: A schematic of the Gly-Gly-His modified PTAA electrode synthesis and its putative complexation with Cu2+(이미지참조). 65
Figure 3.43: Cyclic voltammograms for bare ITO glass (solid line) and PTAA (dash line) between -0.3 and 1.4 V at a scan rate of 10 mV/s. 67
Figure 3.44: ATR-IR spectra for the PTAA electrode (A) and GGH-modified PTAA electrode (B) 67
Figure 3.45: XPS spectra (C1s and N1s (inset)) for PTAA electrode? surface (A) and GGH-modified PTAA electrode (B). (C) XPS spectra (Cu2p) for PTAA electrode (solid line) and GGH-modified PTAA electrode (dash line) following their incubation in Cu2+(이미지참조) solution. 68
Figure 3.46: (A) SWV curves for dissolution of Cu2+ captured by GGH-modified PTAA electrode in the range of 1 - 30 μM Cu2+, (B) SWV peak current for GGH-modified PTAA electrode.(이미지참조) 68
Figure 3.47: (A) SWV curves for dissolution of Cu2+ captured by GGH-modified PTAA electrode in the range of 20 - 700 μM Cu2+, (B(b)) SWV peak current of GGH-modified? PTAA electrode.(이미지참조) 69
Figure 3.48: SWV curves for the Gly-Gly-His modified PTAA electrodes which immersed in different solution for their regeneration 69
Figure 3.49: SWV curves for the Gly-Gly-His modified PTAA electrode incubation in different metal solution 70
Figure 3.50: A schematic of the experiment to assess the binding affinity and/or cross binding affinity of selected Pb2+ binding phages (or peptides) to various metal ions including Pb2+.(이미지참조) 71
Figure 3.51: A relative binding affinity of phage clones selected from chromatographic biopanning, The absorbance is correlated with the amount of phage particles captured by immbolized Pb2+(이미지참조). 72
Figure 3.52: A relative binding afflnity of phage clones selected from chromatographic biopanning, The absorbance is correlated with the amount of phage particles captured by immbolized Pb2+(이미지참조). 73
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