Expulsion of bovine serum albumin from the air/water interface by a sparingly soluble lecithin lipid

Phang, Tze-Lee; Franses, Elias I.

doi:10.1016/j.jcis.2004.02.088

Cited by 16 publications

(34 citation statements)

References 37 publications

(70 reference statements)

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“…The lowest minimum surface tensions, about 2 mN/m, were observed at X = 0.5 for 1212RAc/DMPC. When the measured minimum surface tension was below 5 mN/m, substantial gravity-induced bubble deformation was observed, as reported previously [31,43,44]. The dynamic surface tension maxima, max (not shown) were quite high, ranging from 72 to 70 mN/m for surfactants and from 72 to 60 mN/m for the phospholipids.…”

Section: Dynamic Surface Tensions At Pulsating Area Conditionssupporting

confidence: 81%

Surface tension and adsorption behavior of mixtures of diacyl glycerol arginine-based surfactants with DPPC and DMPC phospholipids

Lozano¹,

Pinazo²,

Pérez³

et al. 2009

Colloids and Surfaces B: Biointerfaces

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Section: Dynamic Surface Tensions At Pulsating Area Conditionssupporting

confidence: 81%

Surface tension and adsorption behavior of mixtures of diacyl glycerol arginine-based surfactants with DPPC and DMPC phospholipids

Lozano¹,

Pinazo²,

Pérez³

et al. 2009

Colloids and Surfaces B: Biointerfaces

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“…Exclusion of albumin and FB from the air/water interface by sodium myristate was demonstrated by McClellan and Franses [15] and Hernandez et al [5]. Expulsion of albumin from the air/water interface by dilauroylphosphatidylcholine (DLPC), which is a sparingly soluble lecithin lipid homologue of DPPC, was reported recently by Phang and Franses [16]. Possible reasons that DLPC tends to expel albumin from the surface are that DLPC produces lower surface energy than albumin and the molecular adsorption allows easy formation of a lipid monolayer of sufficiently low surface energy.…”

Section: Introductionmentioning

confidence: 90%

“…Liu and Chang found that the dynamic tension lowering activity of DPPC can be inhibited by FB [9]. There have been several recent publications on desorption or expulsion of serum proteins by various surfactants or lipids [10][11][12][13][14][15][16], which is analogous to the Vroman effect which involves expulsion of the initially adsorbed protein by another [17,18]. The expulsion of albumin by lipid Langmuir monolayers spread via an organic solvent has been documented by Teneva et al [10], Patino and Nino [11], Cho et al [12], Wen and Franses [8], and Kim and Franses [13].…”

Section: Introductionmentioning

confidence: 99%

Competitive adsorption of fibrinogen and dipalmitoylphosphatidylcholine at the air/aqueous interface

Kim

Franses

2006

Journal of Colloid and Interface Science

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“…This is because the phase of chiral VSFG signals from bulk is different by 90°from that of signals from the interface in the dipole approximation. 42 The VSFG electric fields from the bulk and an interface are expressed as ẼS FG,bulk = r bulk χ bulk (2) Ẽ1Ẽ2 and ẼS FG,interface = ir interface χ interface (2) E1E2, respectively, where r are positive real constants and E1 and E2 are the electric fields of the visible and infrared lasers. Because our reference was the SFG signal of z-cut quartz, ES FG,quartz , which originates from the bulk, signals from bulk and interface are normalized in the analysis procedure as follows, χ eff,bulk (2) = (ES FG,bulk /ES FG,quartz )χ quartz (2) and The Journal of Physical Chemistry C Article χ eff,interface…”

Section: ■ Experimental Sectionmentioning

confidence: 99%

“…5 So far, many studies of proteins at various interfaces have been performed by using homodyne-detected VSFG, and molecular level insight has been obtained. 6−12 Recently, VSFG has been extended to the heterodyne detection scheme, which enables us to determine the phase of the second-order nonlinear susceptibility, χ (2) . 13 −15 The phase carries the information on the polar molecular orientation.…”

Section: ■ Introductionmentioning

confidence: 99%

Heterodyne-Detected Achiral and Chiral Vibrational Sum Frequency Generation of Proteins at Air/Water Interface

Okuno

Ishibashi

2015

J. Phys. Chem. C

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We present complex achiral and chiral vibrational sum frequency generation (VSFG) spectra at the air/ water interface of protein solutions by using heterodynedetected VSFG. Bovine serum albumin, pepsin, concanavalin A, and α-chymotrypsin were measured as model proteins. The obtained achiral Im[χ (2) ] spectra gave us insights into the molecular orientation of protein molecules and water at the interface. From the chiral Im[χ (2) ] spectra in the NH stretching and amide I regions, the secondary structures of the interfacial proteins were deduced. We attributed the chiral signals in the amide I and NH stretching regions to the interface on the basis of the phase of the signals. All the achiral and chiral spectra in each region showed the same sign despite different secondarystructure contents of the examined proteins. Real-time observation of the spectral change of α-chymotrypsin was also performed by heterodyne-detected chiral VSFG. The signal intensity of the chiral Im[χ (2) ] spectra in the NH stretching and amide I regions decreased on the scale of 10 min, originating from the decrease of the portion of antiparallel β-sheet conformation in the molecule. The conformational change occurred not in the bulk but at the interface. Heterodyne-detected achiral and chiral VSFG are capable of addressing the molecular orientation and conformation of proteins at air/water interfaces. ■ INTRODUCTIONIn living organisms, most of the intracellular enzymic processes occur at phase boundaries, that is, the membrane−water interface. At interfaces, protein molecules change their conformation and molecular orientation from those in bulk and then function properly. Understanding the molecular functionality of proteins in living systems requires gaining information not only on bulk but also on interfacial properties. In technological applications, the characterization of interfacial proteins at the molecular level is essential for developing functioning biomaterials such as biocatalysis and biosensors. Thus, determination of secondary structure and molecular orientation of proteins at interfaces is highly important to understand and control the function of proteins. However, there are few methods that investigate interfacial proteins in situ without staining, 1−4 while the tools for studying their properties in bulk have been well established.Vibrational sum frequency generation (VSFG) spectroscopy is suited for studying molecules adsorbed at interfaces. VSFG is a second-order nonlinear spectroscopy, which provides us vibrational spectra reflecting molecular structure with high surface specificity. 5 So far, many studies of proteins at various interfaces have been performed by using homodyne-detected VSFG, and molecular level insight has been obtained. 6−12 Recently, VSFG has been extended to the heterodyne detection scheme, which enables us to determine the phase of the second-order nonlinear susceptibility, χ (2) . 13−15 The phase carries the information on the polar molecular orientation. Contrastingly, in the conventional homod...

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Expulsion of bovine serum albumin from the air/water interface by a sparingly soluble lecithin lipid

Cited by 16 publications

References 37 publications

Surface tension and adsorption behavior of mixtures of diacyl glycerol arginine-based surfactants with DPPC and DMPC phospholipids

Surface tension and adsorption behavior of mixtures of diacyl glycerol arginine-based surfactants with DPPC and DMPC phospholipids

Competitive adsorption of fibrinogen and dipalmitoylphosphatidylcholine at the air/aqueous interface

Heterodyne-Detected Achiral and Chiral Vibrational Sum Frequency Generation of Proteins at Air/Water Interface

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