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Synchrotron FTIR spectroscopy reveals molecular changes in Escherichia coli upon Cu^2+ exposure 被引量:1

Synchrotron FTIR spectroscopy reveals molecular changes in Escherichia coli upon Cu^(2+) exposure
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摘要 Copper ions(e.g.,Cu^(2+)) have outstanding antibacterial properties,but the exact mechanism is rather complex and not fully understood.In this work,synchrotron Fourier transform infrared(FTIR) spectroscopy was used as an analytical tool to investigate the CuCl_2-induced biochemical changes in Escherichia coli.Our spectral measurements indicated that this technique is sensitive enough to detect changes in membrane lipids,nucleic acids,peptidoglycans and proteins of Cu^(2+)-treated bacteria.Interestingly,for short-time treated cells,the effects on phospholipid composition were clearly shown,while no significant alterations of proteins,nucleic acids and peptidoglycans were found.PeakForce quantitative nano-mechanics mode atomic force microscopy(AFM)confirmed the changes in the topography and mechanical properties of bacteria upon the Cu^(2+) exposure.This study demonstrated that FTIR spectroscopy combined with AFM can provide more comprehensive evaluation on the biochemical and mechanical responses of bacteria to copper. Copper ions(e.g.,Cu^2+) have outstanding antibacterial properties,but the exact mechanism is rather complex and not fully understood.In this work,synchrotron Fourier transform infrared(FTIR) spectroscopy was used as an analytical tool to investigate the CuCl2-induced biochemical changes in Escherichia coli.Our spectral measurements indicated that this technique is sensitive enough to detect changes in membrane lipids,nucleic acids,peptidoglycans and proteins of Cu^2+-treated bacteria.Interestingly,for short-time treated cells,the effects on phospholipid composition were clearly shown,while no significant alterations of proteins,nucleic acids and peptidoglycans were found.PeakForce quantitative nano-mechanics mode atomic force microscopy(AFM)confirmed the changes in the topography and mechanical properties of bacteria upon the Cu^2+ exposure.This study demonstrated that FTIR spectroscopy combined with AFM can provide more comprehensive evaluation on the biochemical and mechanical responses of bacteria to copper.
出处 《Nuclear Science and Techniques》 SCIE CAS CSCD 2016年第3期45-52,共8页 核技术(英文)
基金 Supported by National Natural Science Foundation of China(No.11474298) Shanghai Pujiang Program(No.13PJ1410500) Special Funds for Enterprise Independent Innovation of Shanghai(CXY-2013-58) Hundred Talents Program of the Chinese Academy Sciences
关键词 CUCL2 红外光谱 大肠杆菌 同步 原子力显微镜 FTIR光谱 分子 曝光 Copper ions Antibacterial effect Escherichia coli Synchrotron FTIR spectroscopy Atomic force microscopy
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  • 1Miyazawa T, Shimanouchi T, Mizushima S. Characteristic infrared bands of monosubstituted amides. J Chem Phys 1956, 24:408
  • 2Kauppinen JK, Moffatt DJ, Mantsch HH, Cameron DG. Fourier selfdeconvolution: A method for resolving intrinsically overlapped bands. Appl Spectrosc 1986, 35:271-276
  • 3Lee DC, Haris PI, Chapman D, Mitchell RC. Determination of protein secondary structure using factor analysis of infrared spectra. Biochemistry 1990, 29:9185-9193
  • 4Sarver RW, Krueger WC. Protein secondary structure from fourier transform infrared spectroscopy: A data base analysis. Anal Biochem 1991, 194: 89- 100
  • 5Griffiths PR, deHaseth JA. Fourier Transform Infrared Spectroscopy. Wiley Interscience: New York 1986
  • 6Koenig JK, Tabb DL. Analytical Application of FT-IR to Molecular and Biological Systems. D. Reidel: Boston 1980
  • 7Holloway PW, Mantsch HH. Structure of cytochrome b5 in solution by Fourier-transform infrared spectroscopy. Biochemistry 1989, 28:931-935
  • 8Chou PY, Fasman GD. β-turns in proteins. J Mol Biol 1977, 115:135-175
  • 9Susi H, Timasheff SN, Stevens L. Infrared spectra and protein conformations in aqueous solutions. I. The amide I band in H2O and D2O solutions. J Biol Chem 1967, 242:5460-5466
  • 10Gorga JC, Dong A, Manning MC, Woody RW, Caughey WS, Strominger JL. Comparison of the secondary structures of human class Ⅰ and class Ⅱ major histocompatibility complex antigens by Fourier transform infrared and circular dichroism spectroscopy. Proc Natl Acad Sci USA 1989, 86: 2321-2325

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