Abstract
Water confined on nanometer-length scales is found in many physical and biological environments. Confinement induces special dynamics in liquids, different from that of their bulk counterparts. Reverse micelles, formed by the self-assembly of amphiphilic surfactants in nonpolar solvents, have emerged as an appropriate molecular assembly to monitor the property of water upon confinement due to a number of reasons. A unique advantage of reverse micelles is that molecular dynamics can be monitored with varying states of hydration that is difficult to achieve with assemblies, such as membranes. In this article, we focus on the change in confined hydration dynamics accompanied with increasing hydration, monitored by red edge excitation shift (REES). REES can be effectively used to directly monitor the environment and dynamics around a fluorophore in a molecular assembly utilizing slow solvent relaxation around an excited state fluorophore. It is apparent from the examples discussed that change in solvent relaxation with hydration is complicated and could depend on a number of factors, such as the location of the probe in the reverse micelle and the structure and compactness of the fluorophore involved. We conclude that care should be exercised in interpreting such results.
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Abbreviations
- 12-AS:
-
12-(9-Anthroyloxy)stearic acid
- 2-AS:
-
2-(9-Anthroyloxy)stearic acid
- 6-AS:
-
6-(9-Anthroyloxy)stearic acid
- AOT:
-
Sodium bis(2-ethylhexyl)sulfosuccinate
- EGFP:
-
Enhanced green fluorescent protein
- GFP:
-
Green fluorescent protein
- NBD:
-
7-Nitrobenz-2-oxa-1,3-diazol-4-yl
- NBD-cholesterol:
-
25-[N-[(7-nitrobenz-2-oxa-1,3-diazol-4-yl)-methyl]amino]-27-norcholesterol
- NBD-PE:
-
N-(7-nitrobenz-2-oxa-1,3-diazol-4-yl)-1,2-dipalmitoyl-sn-glycero-3-phosphoethanolamine
- REES:
-
Red edge excitation shift
References
Abbyad P, Childs W, Shi X, Boxer SG (2007) Dynamic Stokes shift in green fluorescent protein variants. Proc Natl Acad Sci USA 104:20189–20194
Abel S, Waks M, Urbach W, Marchi M (2006) Structure, stability, and hydration of a polypeptide in AOT reverse micelles. J Am Chem Soc 128:382–383
Abrams FS, Chattopadhyay A, London E (1992) Determination of the location of fluorescent probes attached to fatty acids using the parallax analysis of fluorescence quenching: effect of carboxyl ionization state and environment on depth. Biochemistry 31:5322–5327
Abrams FS, London E (1993) Extension of the parallax analysis of membrane penetration depth to the polar region of model membranes: use of fluorescence quenching by a spin-label attached to the phospholipid polar headgroup. Biochemistry 32:10826–10831
Andrade SM, Costa SM, Pansu R (2000) The influence of water on the photophysical and photochemical properties of Piroxicam in AOT/iso-octane/water reversed micelles. Photochem Photobiol 71:405–412
Bizzarri AR, Cannistraro S (2002) Molecular dynamics of water at the protein–solvent interface. J Phys Chem B 106:6617–6633
Behera GB, Mishra BK, Behera PK, Panda M (1999) Fluorescent probes for structural and distance effect studies in micelles, reversed micelles and microemulsions. Adv Colloid Interface Sci 82:1–42
Bertorelle F, Dondon R, Fery-Forgues S (2002) Compared behavior of hydrophobic fluorescent NBD probes in micelles and in cyclodextrins. J Fluoresc 12:205–207
Bhattacharyya K, Bagchi B (2000) Slow dynamics of constrained water in complex geometries. J Phys Chem A 104:10603–10613
Brubach J-B, Mermet A, Filabozzi A, Gerschel A, Lairez D, Krafft MP, Roy P (2001) Dependence of water dynamics upon confinement size. J Phys Chem B 105:430–435
Chattopadhyay A (1990) Chemistry and biology of N-(7-nitrobenz-2-oxa-1,3-diazol-4-yl)-labeled lipids: fluorescent probes of biological and model membranes. Chem Phys Lipids 53:1–15
Chattopadhyay A (2003) Exploring membrane organization and dynamics by the wavelength-selective fluorescence approach. Chem Phys Lipids 122:3–17
Chattopadhyay A, London E (1987) Parallax method for direct measurement of membrane penetration depth utilizing fluorescence quenching by spin-labeled phospholipids. Biochemistry 26:39–45
Chattopadhyay A, London E (1988) Spectroscopic and ionization properties of N-(7-nitrobenz-2-oxa-1,3-diazol-4-yl)-labeled lipids in model membranes. Biochim Biophys Acta 938: 24–34
Chattopadhyay A, Mukherjee S (1993) Fluorophore environments in membrane-bound probes: a red edge excitation shift study. Biochemistry 32:3804–3811
Chattopadhyay A, Mukherjee S (1999) Depth-dependent solvent relaxation in membranes: wavelength-selective fluorescence as a membrane dipstick. Langmuir 15:2142–2148
Chattopadhyay A, Mukherjee S (1999) Red edge excitation shift of a deeply embedded membrane probe: implications in water penetration in the bilayer. J Phys Chem B 103:8180–8185
Chattopadhyay A, Mukherjee S, Raghuraman H (2002) Reverse micellar organization and dynamics: a wavelength-selective fluorescence approach. J Phys Chem B 106:13002–13009
Cohen B, Huppert D, Solntsev KM, Tsfadia Y, Nachliel E, Gutman M (2002) Excited state proton transfer in reverse micelles. J Am Chem Soc 124:7539–7547
Colombo MF, Rau DC, Parsegian VA (1992) Protein solvation in allosteric regulation: a water effect on hemoglobin. Science 256:655–659
De TK, Maitra A (1995) Solution behaviour of aerosol OT in non-polar solvents. Adv Colloid Interface Sci 59:95–193
Demchenko AP (2002) The red-edge effects: 30 years of exploration. Luminescence 17: 19–42
Demchenko AP (2008) Site-selective red-edge effects. Methods Enzymol 450:59–78
Eastoe J, Young WK, Robinson BH, Steytier DC (1990) Scattering studies of microemulsions in low-density alkanes. J Chem So Faraday Trans 86:2883–2889
Faeder J, Ladanyi BM (2000) Molecular dynamics simulations of the interior of aqueous reverse micelles. J Phys Chem B 104:1033–1046
Fenimore PW, Frauenfelder H, McMohan BH, Parak FG (2002) Slaving: solvent fluctuations dominate protein dynamics and function. Proc Natl Acad Sci USA 99:16047–16051
Fery-Forgues S, Fayet J-P, Lopez A (1993) Drastic changes in the fluorescence properties of NBD probes with the polarity of the medium: involvement of a TICT state? J Photochem Photobiol A 70:229–243
Granick S (1991) Motions and relaxations of confined liquids. Science 253:1374–1379
Haldar S, Chattopadhyay A (2007) Dipolar relaxation within the protein matrix of the green fluorescent protein: a red edge excitation shift study. J Phys Chem B 111:14436–14439
Haldar S, Raghuraman H, Chattopadhyay A (2008) Monitoring orientation and dynamics of membrane-bound melittin utilizing dansyl fluorescence. J Phys Chem B 112:14075–14082
Haldar S, Chattopadhyay A (2009) The green journey. J Fluoresc 19:1–2
Haldar S, Chattopadhyay A (2009) Green fluorescent protein: a molecular lantern that illuminates the cellular interior. J Biosci 34:169–172
Häussinger D (1996) The role of cellular hydration in the regulation of cell function. Biochem J 313:697–710
Hazra P, Sarkar N (2001) Intramolecular charge transfer processes and solvation dynamics of coumarin 490 in reverse micelles. Chem Phys Lett 342:303–311
Hof M, Lianos P, Laschewsky A (1997) An amphiphilic hemicyanine dye employed as a sensitive probe of water in reverse AOT micelles. Langmuir 13:2181–2183
Ikushima Y, Saito N, Arai M (1997) The nature and structure of water/AOT/ethane (w/o) microemulsion under supercritical conditions studied by high-pressure FT-IR spectroscopy. J Colloid Interface Sci 186:254–263
Israelachvili JN, Marcelja S, Horn RG (1980) Physical principles of membrane organization. Q Rev Biophys 13:121–200
Jain TK, Varshney M, Maitra A (1989) Structural studies of Aerosol OT reverse micellar aggregates by FT-IR spectroscopy. J Phys Chem 93:7409–7416
Kelkar DA, Chattopadhyay A (2004) Depth-dependent solvent relaxation in reverse micelles: a fluorescence approach. J Phys Chem B 108:12151–12158
Kelkar DA, Chattopadhyay A (2005) Effect of graded hydration on the dynamics of an ion channel peptide: a fluorescence approach. Biophys J 88:1070–1080
Kelkar DA, Chattopadhyay A (2007) The gramicidin ion channel: a model membrane protein. Biochim Biophys Acta 1768:2011–2025
Ketchem RR, Hu W, Cross TA (1993) High-resolution conformation of gramicidin A in a lipid bilayer by solid-state NMR. Science 261:1457–1460
Lin S, Struve WS (1991) Time-resolved fluorescence of nitrobenzoxadiazole-aminohexanoic acid: effect of intermolecular hydrogen-bonding on non-radiative decay. Photochem Photobiol 54:361–365
Levinger NE (2002) Water in confinement. Science 298:1722–1723
Levinger NE, Swafford LA (2009) Ultrafast dynamics in reverse micelles. Annu Rev Phys Chem 60:385–406
Luisi PL, Magid LJ (1986) Solubilization of enzymes and nucleic acids in hydrocarbon micellar solutions. CRC Crit Rev Biochem 20:409–473
Luisi PL, Giomini M, Pileni MP, Robinson BH (1988) Reverse micelles as hosts for proteins and small molecules. Biochim Biophys Acta 947:209–246
Mattos C (2002) Protein-water interactions in a dynamic world. Trends Biochem Sci 27:203–208
Mazères S, Schram V, Tocanne J-F, Lopez A (1996) 7-Nitrobenz-2-oxa-1,3-diazole-4-yl-labeled phospholipids in lipid membranes: differences in fluorescence behavior. Biophys J 71: 327–335
Melo EP, Aires-Barros MR, Cabral JMS (2001) Reverse micelles and protein biotechnology. Biotechnol Annu Rev 7:87–129
Mentré P (2001) An introduction to “water in the cell”: tamed hydra? Cell Mol Biol 47: 709–715
Mitra B, Hammes GG (1990) Membrane-protein structural mapping of chloroplast coupling factor in asolectin vesicles. Biochemistry 29:9879–9884
Moilanen DE, Fenn EE, Wong D, Fayer MD (2009) Geometry and nanolength scales versus interface interactions: water dynamics in AOT lamellar structures and reverse micelles. J Am Chem Soc 131:8318–8328
Mukherjee S, Chattopadhyay A (1994) Motionally restricted tryptophan environments at the peptide–lipid interface of gramicidin channels. Biochemistry 33:5089–5097
Mukherjee S, Chattopadhyay A, Samanta A, Soujanya T (1994) Dipole moment change of NBD group upon excitation studied using solvatochromic and quantum chemical approaches: implications in membrane research. J Phys Chem 98:2809–2812
Mukherjee S, Chattopadhyay A (1995) Wavelength-selective fluorescence as a novel tool to study organization and dynamics in complex biological systems. J Fluoresc 5:237–246
Mukherjee S, Chattopadhyay A (1996) Membrane organization at low cholesterol concentrations: a study using 7-nitrobenz-2-oxa-1,3-diazol-4-yl-labeled cholesterol. Biochemistry 35:1311–1322
Mukherjee S, Kalipatnapu S, Pucadyil TJ, Chattopadhyay A (2006) Monitoring the organization and dynamics of bovine hippocampal membranes utilizing differentially localized fluorescent membrane probes. Mol Membr Biol 23:430–441
Papoian GA, Ulander J, Eastwood MP, Luthey-Schulten Z, Wolynes PG (2004) Water in protein structure prediction. Proc Natl Acad Sci USA 101:3352–3357
Park S, Moilanen DE, Fayer MD (2008) Water dynamics – the effects of ions and nanoconfinement. J Phys Chem B 112:5279–5290
Pucadyil TJ, Mukherjee S, Chattopadhyay A (2007) Organization and dynamics of NBD-labeled lipids in membranes analyzed by fluorescence recovery after photobleaching. J Phys Chem B 111:1975–1983
Raghuraman H, Chattopadhyay A (2003) Organization and dynamics of melittin in environments of graded hydration: a fluorescence approach. Langmuir 19:10332–10341
Raghuraman H, Chattopadhyay A (2006) Effect of ionic strength on folding and aggregation of the hemolytic peptide melittin in solution. Biopolymers 83:111–121
Raghuraman H, Chattopadhyay A (2007) Melittin: a membrane-active peptide with diverse functions. Biosci Rep 27:189–223
Raghuraman H, Kelkar DA, Chattopadhyay A (2005) Novel insights into protein structure and dynamics utilizing the red edge excitation shift approach. In: Geddes CD, Lakowicz JR (eds) Reviews in fluorescence, vol 2. Springer, New York, pp 199–214
Rawat SS, Chattopadhyay A (1999) Structural transition in the micellar assembly: a fluorescence study. J Fluoresc 9:233–244
Rukmini R, Rawat SS, Biswas SC, Chattopadhyay A (2001) Cholesterol organization in membranes at low concentrations: effects of curvature stress and membrane thickness. Biophys J 81:2122–2134
Samanta A (2006) Dynamic Stokes shift and excitation wavelength dependent fluorescence of dipolar molecules in room temperature ionic liquids. J Phys Chem B 110:13704–13716
Sarkar N, Das K, Datta A, Das S, Bhattacharyya K (1996) Solvation dynamics of coumarin 480 in reverse micelles. Slow relaxation of water molecules. J Phys Chem 100:10523–10527
Sarkar M, Ray JG, Sengupta PK (1996) Luminescence behaviour of 7-hydroxyflavone in aerosol OT reverse micelles: excited-state proton transfer and red-edge excitation effects. J Photochem Photobiol A 95:157–160
Saxena AM, Udgaonkar JB, Krishnamoorthy G (2005) Protein dynamics control proton transfer from bulk solvent to protein interior: a case study with a green fluorescent protein. Protein Sci 14:1787–1789
Souto AL, Ito AS (2000) Tryptophan fluorescence studies of melanotropins in the amphiphile-water interface of reversed micelles. Eur Biophys J 29:38–47
Tanford C (1978) The hydrophobic effect and the organization of living matter. Science 200:1012–1018
Tanford C (1980) The hydrophobic effect: formation of biological membranes. Wiley, New York
Tanford C (1987) Amphiphile orientation: physical chemistry and biological function. Biochem Soc Trans 15:1S–7S
Timasheff SN (2002) Protein hydration, thermodynamic binding and preferential hydration. Biochemistry 41:13473–13482
Tsien RY (1998) The green fluorescent protein. Annu Rev Biochem 67:509–544
Valdez D, Le Huérou J-Y, Gindre M, Urbach W, Waks M (2001) Hydration and protein folding in water and in reverse micelles: compressibility and volume changes. Biophys J 80:2751–2760
Venables DS, Huang K, Schmuttenmaer CA (2001) Effect of reverse micelle size on the librational band of confined water and methanol. J Phys Chem B 105:9132–9138
Villaín J, Prieto M (1991) Location and interaction of N-(9-anthroyloxy)-stearic acid probes incorporated in phosphatidylcholine vesicles. Chem Phys Lipids 59:9–16
Wolf DE, Winiski AP, Ting AE, Bocian KM, Pagano RE (1992) Determination of the transbilayer distribution of fluorescent lipid analogues by nonradiative fluorescence energy transfer. Biochemistry 31:2865–2873
Wyttenbach T, Bowers MT (2009) Hydration of biomolecules. Chem Phys Lett 480:1–16
Xu F, Cross TA (1999) Water: foldase activity in catalyzing polypeptide conformational rearrangements. Proc Natl Acad Sci USA 96:9057–9061
Acknowledgments
Work in A.C.’s laboratory was supported by the Council of Scientific and Industrial Research and Department of Science and Technology, Government of India. S.H. thanks the Council of Scientific and Industrial Research for the award of a Senior Research Fellowship. A.C. is an Adjunct Professor at the Special Centre for Molecular Medicine of Jawaharlal Nehru University (New Delhi, India) and Honorary Professor of the Jawaharlal Nehru Centre for Advanced Scientific Research (Bangalore, India). A.C. gratefully acknowledges J.C. Bose Fellowship (Department of Science and Technology, Government of India). Some of the work described in this article was carried out by former members of A.C.’s group whose contributions are gratefully acknowledged. We thank Arunima Chaudhuri for help with Fig. 1 and members of our laboratory for critically reading the manuscript.
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Haldar, S., Chattopadhyay, A. (2012). Hydration Dynamics of Probes and Peptides in Captivity. In: Geddes, C. (eds) Reviews in Fluorescence 2010. Reviews in Fluorescence, vol 2010. Springer, New York, NY. https://doi.org/10.1007/978-1-4419-9828-6_7
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