Interactions between plasma proteins and pulmonary surfactant: pulsating bubble studies

1989 ◽  
Vol 67 (6) ◽  
pp. 663-668 ◽  
Author(s):  
Kevin M. W. Keough ◽  
Caroline S. Parsons ◽  
Martin G. Tweeddale
Keyword(s):  
Surface Tension ◽  
Plasma Proteins ◽  
Pulmonary Surfactant ◽  
Distress Syndrome ◽  
Adsorption Process ◽  
Human Albumin ◽  
Water Interface ◽  
Dipalmitoyl Phosphatidylcholine ◽  
Air Water Interface ◽  
Surfactant Inhibition

The influence of human albumin, α-globulin, and fibrinogen on the actions of porcine pulmonary surfactant in a pulsating bubble surfactometer has been investigated. All three proteins detracted from the ability of the surfactant to adsorb to the air–water interface. The proteins also reduced the ability of surfactant to lower the opening pressures of bubbles cycling between different sizes in suspensions of surfactant. This was equivalent to restricting the ability of the surfactant to achieve low surface tension during compression of the surface. Of the three proteins, globulin competed most effectively with surfactant during the adsorption process, and albumin competed the least effectively. The proteins also may have interfered with the processes of surface refinement, which usually yields a monolayer enriched enough in dipalmitoyl phosphatidylcholine to achieve very low surface tension (very low opening pressures in the bubbles). Of the three proteins tested, albumin was least deleterious to surface refining whereas globulin and fibrinogen appeared to be about equally detrimental to the process.Key words: pulmonary surfactant, surface tension, adsorption, adult respiratory distress syndrome, surfactant inhibition.

From Surface Tension to Molecular Distribution: Modeling Surfactant Adsorption at the Air–Water Interface

Langmuir ◽  
2021 ◽  
Vol 37 (7) ◽  
pp. 2237-2255 ◽  
Author(s):  
Mengsu Peng ◽  
Timothy T. Duignan ◽  
Cuong V. Nguyen ◽  
Anh V. Nguyen
Keyword(s):  
Surface Tension ◽  
Surfactant Adsorption ◽  
Water Interface ◽  
Molecular Distribution ◽  
Distribution Modeling ◽  
Air Water Interface

Surface active properties at the air–water interface of β-casein and its fragments derived by plasmin proteolysis

1989 ◽  
Vol 56 (3) ◽  
pp. 487-494 ◽  
Author(s):  
Michael Wilson ◽  
Daniel M. Mulvihill ◽  
William J. Donnelly ◽  
Brian P. Gill
Keyword(s):  
Surface Tension ◽  
Water Interface ◽  
Active Protein ◽  
Drop Volume ◽  
V Protein ◽  
Proteose Peptone ◽  
Rate Determining Step ◽  
Surface Active Properties ◽  
Air Water Interface ◽  
Surface Active

Summaryβ-Casein, was enzymically modified by incubation with plasmin to yield γ-caseins and proteose peptones. Whole γ-, γ1-, γ2/γ3-caseins and whole proteose peptone (pp) were isolated from the hydrolysate mixture. The time dependence of surface tension at the air-water interface of solutions of β-casein and its plasmin derived fragments, at concentrations of 10−1 to 10−4% (w/v) protein, pH 7.0, was determined, at 25 °C, using a drop volume apparatus. The ranking of the proteins with respect to rate of reduction of surface tension, during the first rate determining step, at 10-2% (w/v) protein, was γ2/γ3 ≫ pp > whole γ- > γ1- > β-casein. The ranking of the proteins with respect to surface pressures attained after 40 min (π40) was concentration dependent. γ2/γ3-Caseins were found to be very surface active, decreasing surface tension rapidly and giving a high π40. γ1 Casein decreased surface activity somewhat faster than β-casein, but generally reached a lower π40. Whole γ-casein reflected the properties of both γ1 and γ2/γ3-caseins. Proteose peptone was found to decrease surface tension rapidly during the initial rate determining step; it gave a relatively high π40 at a bulk phase concentration of 10−3% (w/v) protein, but, it was the least surface active protein at 10−1 and 10−2% (w/v) protein.

scholarly journals Effect of a surface tension gradient on the slip flow along a superhydrophobic air-water interface

2018 ◽  
Vol 3 (3) ◽  
Author(s):  
Dong Song ◽  
Baowei Song ◽  
Haibao Hu ◽  
Xiaosong Du ◽  
Peng Du ◽  
...  
Keyword(s):  
Surface Tension ◽  
Slip Flow ◽  
Surface Tension Gradient ◽  
Water Interface ◽  
Air Water Interface

Temperature dependence of dipalmitoyl phosphatidylcholine monolayer stability

1981 ◽  
Vol 51 (5) ◽  
pp. 1108-1114 ◽  
Author(s):  
J. Goerke ◽  
J. Gonzales
Keyword(s):  
Phase Transition ◽  
Lung Surfactant ◽  
Principal Component ◽  
Water Interface ◽  
Dipalmitoyl Phosphatidylcholine ◽  
Phase Transition Temperatures ◽  
Air Water Interface ◽  
Different Temperatures ◽  
Monolayer Stability ◽  
Isolated Rat

Dipalmitoyl phosphatidylcholine is the principal component of lung surfactant, and knowledge of its behavior as a film spread at the air-water interface is essential for understanding how lung surfactant itself works. We therefore studied the collapse rates of very low surface tension air-water monolayers of dipalmitoyl, dimyristoyl, and palmitoyl-myristoyl phosphatidylcholines at different temperatures. In each case we found that the monolayers abruptly became unstable at temperature 3–4 degree C above their bulk lipid-water phase transition temperatures (Tc). This accords with a comparable increase in Tc occurring in bulk systems subjected to high pressure. These findings are also consistent with the behavior of isolated rat lungs, which have been found to require higher transmural pressures to maintain a given volume on deflation when kept at temperature above the Tc of dipalmitoyl phosphatidylcholine.

Observations on the locomotion of post-larval and juvenile flying fish

1990 ◽  
Vol 70 (2) ◽  
pp. 311-320 ◽  
Author(s):  
John Davenport
Keyword(s):  
Surface Tension ◽  
Surface Roughness ◽  
Reynolds Numbers ◽  
Maximum Speed ◽  
Tail Flick ◽  
Horizontal Distance ◽  
Water Interface ◽  
Flying Fish ◽  
Air Water Interface ◽  
Air Penetration

Post-larval specimens of Hirundichthys affinis are capable of jumping out of water, but the pectoral and pelvic fins are not extended when in air. Penetration through the air/ water interface demands a force to overcome surface tension which is similar in magnitude to the force required for the jump itself. However, post-larvae do not produce the single propulsive tail flick which powers the jump until most of the animal has passed through the interface. The post-larva emerges at an angle close to 45°, thus maximising the horizontal distance travelled before re-entry.Whether swimming slowly (4 body lengths s-1), or at maximum speed (36 body lengths s-1), post-larvae swim with the pectoral and pelvic fins extended. Calculations show that fast swimming post-larvae operate at Reynolds’ numbers of about 4×103, where surface roughness and projections decrease rather than increase drag.

Influence of pH on the surface and foaming properties of aqueous silk fibroin solutions

Soft Matter ◽  
2020 ◽  
Vol 16 (15) ◽  
pp. 3695-3704 ◽  
Author(s):  
Xiuying Qiao ◽  
Reinhard Miller ◽  
Emanuel Schneck ◽  
Kang Sun
Keyword(s):  
Surface Tension ◽  
Silk Fibroin ◽  
Bubble Coalescence ◽  
Foaming Properties ◽  
Water Interface ◽  
Interfacial Layers ◽  
Air Water Interface ◽  
Influence Of Ph

Silk fibroin (SF) adsorbs at the air/water interface, reduces the surface tension, and forms interfacial layers suppressing bubble coalescence and stabilizing foam.

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