Pressure-induced phase transitions of lipid bilayers observed by fluorescent probes Prodan and Laurdan

Kusube, Masataka; Tamai, Naoto; Matsuki, Hitoshi; Kaneshina, Shoji

doi:10.1016/j.bpc.2005.05.007

Cited by 34 publications

(21 citation statements)

References 39 publications

(36 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…In contrast, at low a hh , the head-head contacts become favorable, water is expelled from the head group region, the resulted smaller area per lipid drive the tails more ordered and straighter, consequently the L β phase is evolved. It is worthy to note that the phase diagrams in Figure 10 do not include any interdigitated phases, although they were found in several systems experimentally [75,[77][78][79][80]. Inspired by the results from the single-tail lipids that the interdigitated phase could be stabilize by increasing distance between neighboring head groups, Smit's group built an ingenious approach to locate them.…”

Section: D Phase Transformation In Lipid Bilayermentioning

confidence: 96%

“…The transition from the sub-gel phase to the gel phase is generally called as subtransition. If head groups are large and weakly interacted, such as ether-linked phosphatidyl-cholines, the system adopts a L βI phase (Figure 8(c)), where both opposing lipid layers are fully interdigitated [75,[77][78][79][80]. On the one hand, both L β# and L C phases are characterized by having a very low lipid mobility in the bilayer plane accompanied with the ordered tail chains, which can also be tilted with respect to the lipid bilayer normal.…”

Section: D Phase Transformation In Lipid Bilayermentioning

confidence: 99%

See 1 more Smart Citation

Dissipative particle dynamic simulation study of lipid membrane

Guo

2010

Front. Chem. China

View full text Add to dashboard Cite

The lipid membrane plays crucial roles in countless biologic processes, ranging from cell motility, endo-and exocytosis, and cell division to protein aggregation and trafficking. To gain a molecular insight in these biologic processes, the recently developed mesoscale simulation technique, dissipative particle dynamics (DPD) simulation, has become an invaluable tool. By providing a brief survey of existing atomistic and popular coarse-grained models used today in studying the dynamics (including vesicle formation and (protein-mediated) vesicle fusion) and phase behavior of lipid bilayers, this review illustrates how mesoscopic DPD models can be used to obtain a better understanding of these biologic processes currently inaccessible to atomistic and most coarse-grained models.

show abstract

Section: D Phase Transformation In Lipid Bilayermentioning

confidence: 96%

Section: D Phase Transformation In Lipid Bilayermentioning

confidence: 99%

Dissipative particle dynamic simulation study of lipid membrane

Guo

2010

Front. Chem. China

View full text Add to dashboard Cite

show abstract

“…Fluorescent probes such as prodan (6-propionyl-2-dimethylaminonaphthalene) and laurdan (6-dodecanoyl-2-dimethylaminonaphthalene) are widely used in biological and biophysical research [1][2][3][4][5][6][7][8][9][10][11][12][13][14][15]. The fluorescence properties of prodan and laurdan have been described in the literature as simultaneously existing local-excited (LE) and twisted internal charge-transfer (TICT) states.…”

Section: 37mentioning

confidence: 99%

Effect of proton-donor solvent and structural flexibility of prodan and laurdan molecules on their spectral-luminescent properties

et al. 2009

View full text Add to dashboard Cite

535.37The influence of structural flexibility on dipole moments, energy-level locations, and charge distributions in prodan and laurdan molecules was studied. A quantum-chemical calculation of isolated prodan and laurdan molecules in the fluorescent state geometry was conducted. Rate constants for radiative and non-radiative processes and fluorescence quantum yields for these probe molecules were calculated. Interaction centers of prodan and laurdan with a proton-donor solvent were estimated quantitatively. The possibility of using fluorescent probes for estimating the polarity of proton-donor and proton-acceptor solvents was shown.Keywords: fluorescent probe, prodan, laurdan, structural flexibility, proton-donor properties, fluorescence quantum yield.Introduction. Fluorescent probes such as prodan (6-propionyl-2-dimethylaminonaphthalene) and laurdan (6-dodecanoyl-2-dimethylaminonaphthalene) are widely used in biological and biophysical research [1][2][3][4][5][6][7][8][9][10][11][12][13][14][15]. The fluorescence properties of prodan and laurdan have been described in the literature as simultaneously existing local-excited (LE) and twisted internal charge-transfer (TICT) states. However, the latter term should be used very arbitrarily because the state has been observed only at very low temperatures [2]. These states are strongly delocalized at temperatures near ambient and above [2]. It has been shown [5] that the positions of fluorescence maxima in phospholipids bilayers depend on the phase state of the phospholipids, i.e., 435 and 440 nm for the short-wavelength band in the gel phase; 515 and 490 nm, for prodan and laurdan in the liquid-crystalline phase. Two fluorescence bands (430 and 500 nm) were observed for laurdan in glycerin with λ ex = 380 nm at room temperature. The short-wavelength band at 430 nm disappeared as the temperature was raised to 370 K.The large shifts of prodan and laurdan fluorescence bands in solvents of different polarity have been explained by the significant change of dipole moment in the excited state as compared with the ground state. According to formulas for calculating common effects of solvents [16,17], changing the prodan dipole moment from 5.5 to 10.2 D causes a shift of the S 0 → S 1 -transition [18,19] in its fluorescence spectra of 770 cm -1 and 800 cm -1 on going to isopropanol and water, respectively, from a non-polar solvent [19,20]. The experimental shifts in fluorescence spectra of prodan were 3790 and 5520 cm -1 in isopropanol and water, i.e., the size of the dipole moment and its change from

show abstract

“…Lateral pressure profiles such as those depicted in Fig. 8 may be obtained from MD simulations [117][118][119], though a recent approach relying on pressure-susceptible fluorescent probes that preferentially localise to different parts of a lipid bilayer holds promise for experimental confirmation [120][121][122][123]. b Addition of lipids with small headgroups, such as POPE, redistributes positive lateral pressure from the headgroup regions to the hydrocarbon core.…”

Section: Physical Originmentioning

confidence: 99%

Protein folding in membranes

Fiedler

Broecker

Keller

2010

Cell. Mol. Life Sci.

View full text Add to dashboard Cite

Separation of cells and organelles by bilayer membranes is a fundamental principle of life. Cellular membranes contain a baffling variety of proteins, which fulfil vital functions as receptors and signal transducers, channels and transporters, motors and anchors. The vast majority of membrane-bound proteins contain bundles of alpha-helical transmembrane domains. Understanding how these proteins adopt their native, biologically active structures in the complex milieu of a membrane is therefore a major challenge in today's life sciences. Here, we review recent progress in the folding, unfolding and refolding of alpha-helical membrane proteins and compare the molecular interactions that stabilise proteins in lipid bilayers. We also provide a critical discussion of a detergent denaturation assay that is increasingly used to determine membrane-protein stability but is not devoid of conceptual difficulties.

show abstract

Pressure-induced phase transitions of lipid bilayers observed by fluorescent probes Prodan and Laurdan

Cited by 34 publications

References 39 publications

Dissipative particle dynamic simulation study of lipid membrane

Dissipative particle dynamic simulation study of lipid membrane

Effect of proton-donor solvent and structural flexibility of prodan and laurdan molecules on their spectral-luminescent properties

Protein folding in membranes

Contact Info

Product

Resources

About