Hücre Zarı Sinyalinin NMR Spektroskopisi ile Belirlenmesi

Year 2018, Volume: 4 Issue: 1, 47 - 50, 25.07.2018

Sibel Korunur Ali Yılmaz

https://doi.org/10.29132/ijpas.359756

Abstract

Hücre zarı, hücrenin
sınırlarını oluşturur ve hücre içi ile dışı arasındaki madde geçişini düzenler.
Hücrenin kendisi için gerekli besin maddelerini
dış ortamdan alıp metabolizma sonucu oluşan zararlı metabolitleri dış ortama
verme olayında hücre zarlarının büyük bir rolü bulunmaktadır. Bu çalışmada sulu çözeltideki bir hücre zarı örneğinin 400 MHz ¹H-NMR spektrumu, tek puls ve
presaturasyon metodu kullanılarak alınmış ve bu iki spektrumun
karşılaştırmasıyla hücre zarı sinyalinin yeri saptanmaya çalışılmıştır.

Keywords

Hücre zarı, nükleer manyetik rezonans, presaturasyon metodu

Determination of Cell Membrane Signal by using NMR Spectroscopy

Abstract

The cell membrane forms the boundaries of the cell and regulates the
passage of matter between the inside and the outside of the cell. Cell
membranes play a major role in the process of taking the necessary nutrients
from the outside and exerting the harmful metabolites resulting from the
metabolism. In this study, 400 MHz ¹H-NMR spectrum of a membrane
sample in an aqueous solution was taken using single pulse and presaturation
method and it has been tried to determine the location of the membrane signal
by comparing these two spectrums.

Keywords

Cell membrane, presaturation method, nuclear magnetic resonance

References

• Abu-Baker, S., Lorigan, G.A., 2012. Solid-State NMR Spectroscopic Approaches to Investigate Dynamics, Secondary Structure and Topology of Membrane Proteins. Open Journal of Biophysics, 2(4):109-116.
• Babcock, J.J., Li, M., 2014. Deorphanization the human transmembrane genome: A landscape of uncharacterized membrane proteins. Acta Pharmacologica Sinica, 35(1):11–23.
• Bull, S.C., Doig, A.J., 2015. Properties of Protein Drug Target Classes. PLoS One., 10(3):1-44.
• Grover, V.P.B., Tognarelli, J.M., Crossey, M.M.E., Cox, I.J., Taylor-Robinson, S.D., McPhail, M.J.W., 2015. Magnetic Resonance Imaging: Principles and Techniques: Lessons for Clinicians. Journal of Clinical and Experimental Hepatology, 5(3):246–255.
• Jao, C., 2005. Basic instructions for Bruker NMR AVANCE 400 Running TOPSPIN, Guide to presaturation experiment for solvent suppression. http://nmr.bc.sinica.edu.tw/instruments/data/NMR/1H_Presaturation.pdf
• Marion, D., 2013. An introduction to biological NMR spectroscopy. Molecular & Cellular Proteomics, 12(11):3006–3025.
• Middleton, D.A., Reid, D.G., Watts, A., 2004. Combined quantitative and mechanistic study of drug–membrane interactions using a novel 2H NMR approach. Journal of Pharmaceutical Sciences, 93(2):507-514.
• Nielsen, N., Malmendal, A., Vosegaard, T., 2004. Techniques and applications of NMR to membrane proteins. Molecular Membrane Biology, 21:129-141.
• Opella, S.J., Ma, C., Marassi, F.M., 2001. Nuclear magnetic resonance of membrane-associated peptides and proteins. Methods in Enzymology, 339:285–313.
• Pignatello, R., Musumeci, T., Basile, L., Carbone, C., Puglisi, G., 2011. Biomembrane models and drug-biomembrane interaction studies: Involvement in drug design and development. Journal of Pharmacy and Bioallied Sciences, 3(1):4–14.
• Schnell, D.J., Hebert, D.N., 2003. Protein translocons: multifunctional mediators of protein translocation across membranes. Cell, 112(4):491-505.
• Tamm, L.K., Liang, B., 2006. NMR of membrane proteins in solution. Progress in Nuclear Magnetic Resonance Spectroscopy, 48:201–210.
• Thennarasu, S., Lee, D., Poon, A., Kawulka, K.E., Vederas, J.C., Ramamoorthy, A., 2005. Membrane permeabilization, orientation and antimicrobial mechanism of subtilosin A. Chemistry and Physics of Lipids, 137:38-51.
• Webb, G.A., 2007. Nuclear Magnetic Resonance, 36. Cilt, Specialist Periodical Reports, Royal Society of Chemistry, Cambridge, UK.
• Wüthrich, K., 1986. NMR of proteins and nucleic acids, Wiley, New York.
• Xu, Y., Yushmanov, V.E., Tang, P., 2002. NMR studies of drug interaction with membranes and membrane-associated proteins. Bioscience Reports, 22:175-190.
• Yilmaz, A., Zengin B., 2013. High-field NMR T2 relaxation mechanism in D2O solutions of albumin. Journal of Applied Spectroscopy, 80 (3):335-340.
• Yilmaz, A, Zengin, B, Ulak, F.S., 2014. NMR proton spin-lattice relaxation mechanism in D2O solutions of albumin determined at 400 MHz. Journal of Applied Spectroscopy, 81(3):365-370.