Liquid-vapor interfacial tension of blood plasma, serum and purified protein constituents thereof.
Abstract: A systematic study of water-air (liquid-vapor, LV) interfacial tension gamma(lv) of blood plasma and serum derived from four different mammalian species (human, bovine, ovine and equine) reveals nearly identical concentration-dependence (dgamma(lv)/dlnC(B); where C(B) is plasma/serum dilution expressed in v/v concentration units). Comparison of results to a previously-published survey of purified human-blood proteins further reveals that dgamma(lv)/dlnC(B) of plasma and serum is surprisingly similar to that of purified protein constituents. It is thus concluded that any combination of blood-protein constituents will be substantially similar because dgamma(lv)/dlnC(B) of individual proteins are very similar. Experimental results are further interpreted in terms of a recently-developed theory emphasizing the controlling role of water in protein adsorption. Accordingly, the LV interphase saturates with protein adsorbed from bulk solution at a fixed weight-volume concentration ( approximately 436 mg/mL) independent of protein identity or mixture. As a direct consequence, dgamma(lv)/dlnC(B) of purified proteins closely resembles that of mixed solutions and does not depend on the relative proportions of individual proteins comprising a mixture. Thus variations in the plasma proteome between species are not reflected in dgamma(lv)/dlnC(B) nor is serum different from plasma in this regard, despite being depleted of coagulation proteins (e.g. fibrinogen). A comparison of pendant-drop and Wilhelmy-balance tensiometry as tools for assessing protein gamma(lv) shows that measurement conditions employed in the typical Wilhelmy plate approach fails to achieve the steady-state adsorption state that is accessible to pendant-drop tensiometry.
Publication Date: 2004-12-29 PubMed ID: 15621233DOI: 10.1016/j.biomaterials.2004.09.016Google Scholar: Lookup
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- Comparative Study
- Evaluation Study
- Journal Article
- Research Support
- N.I.H.
- Extramural
- Research Support
- Non-U.S. Gov't
- Research Support
- U.S. Gov't
- P.H.S.
Summary
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The research article in question conducts a comparative study of water-air interfacial tension in the blood plasma and serum obtained from four different mammal species. Their findings indicate that the concentration-dependence of this tension in plasma and serum is almost the same across all species and even comparable to that in purified blood proteins.
Research Methodology
- The researchers conducted a systematic review of the liquid-vapor (LV), or water-air, interfacial tension (gamma(lv)) in the blood plasma and serum from four different mammalian species: human, bovine (cattle), ovine (sheep), and equine (horse).
- This tension’s concentration-dependence was expressed as dgamma(lv)/dlnC(B), with C(B) representing the plasma/serum dilution in volume/volume concentration units.
- These results were then compared to a previous study that studied gamma(lv) in purified human blood proteins.
Key Findings
- The researchers found that the concentration-dependence (dgamma(lv)/dlnC(B)) of gamma(lv) in plasma and serum is similar across all species. This uniformity implies that the combination of blood-protein constituents does not significantly affect gamma(lv).
- More surprisingly, the same concentration-dependence is also comparable to purified blood proteins’ values.
- The study also theorized that the protein’s absorption at the LV interphase is controlled by the water present and reaches saturation at a fixed weight-volume concentration, unaffected by the protein’s identity or mixture.
- As a result, dgamma(lv)/dlnC(B) doesn’t vary based on the individual proteins in a mixture or the proportions thereof.
- Unlike expectations, the variations between species in plasma proteome, or the total set of proteins, do not reflect in dgamma(lv)/dlnC(B). The same applies to the comparison between serum, which is free of coagulation proteins like fibrinogen, and plasma.
Research Tools and Techniques
- The researchers used pendant-drop tensiometry and Wilhelmy-balance tensiometry to measure the gamma(lv).
- The study concluded that the typical Wilhelmy plate approach didn’t achieve the steady-state adsorption state compared to the pendant-drop tensiometry method.
Cite This Article
APA
Krishnan A, Wilson A, Sturgeon J, Siedlecki CA, Vogler EA.
(2004).
Liquid-vapor interfacial tension of blood plasma, serum and purified protein constituents thereof.
Biomaterials, 26(17), 3445-3453.
https://doi.org/10.1016/j.biomaterials.2004.09.016 Publication
Researcher Affiliations
- Department of Bioengineering, The Pennsylvania State University, 103 Steidle Bldg, University Park, PA 16802-5005, USA.
MeSH Terms
- Animals
- Blood Proteins / analysis
- Blood Proteins / chemistry
- Cattle
- Horses
- Humans
- Phase Transition
- Plasma / chemistry
- Protein Binding
- Serum / chemistry
- Sheep
- Species Specificity
- Surface Tension
Grant Funding
- 5 R01 HL 69965-03 / NHLBI NIH HHS
Citations
This article has been cited 16 times.- Yadav SS, Sikarwar BS, Ranjan P, Janardhanan R. Microfluidic system for screening disease based on physical properties of blood. Bioimpacts 2020;10(3):141-150.
- Manivasagam VK, Popat KC. In Vitro Investigation of Hemocompatibility of Hydrothermally Treated Titanium and Titanium Alloy Surfaces. ACS Omega 2020 Apr 14;5(14):8108-8120.
- Fathi-Azarbayjani A, Jouyban A. Surface tension in human pathophysiology and its application as a medical diagnostic tool. Bioimpacts 2015;5(1):29-44.
- Vogler EA. Protein adsorption in three dimensions. Biomaterials 2012 Feb;33(5):1201-37.
- Josh Yeh CH, Dimachkie ZO, Golas A, Cheng A, Parhi P, Vogler EA. Contact activation of blood plasma and factor XII by ion-exchange resins. Biomaterials 2012 Jan;33(1):9-19.
- Liao Z, Lampe JW, Ayyaswamy PS, Eckmann DM, Dmochowski IJ. Protein assembly at the air-water interface studied by fluorescence microscopy. Langmuir 2011 Nov 1;27(21):12775-81.
- Parhi P, Golas A, Barnthip N, Noh H, Vogler EA. Volumetric interpretation of protein adsorption: capacity scaling with adsorbate molecular weight and adsorbent surface energy. Biomaterials 2009 Dec;30(36):6814-24.
- Barnthip N, Parhi P, Golas A, Vogler EA. Volumetric interpretation of protein adsorption: kinetics of protein-adsorption competition from binary solution. Biomaterials 2009 Nov;30(33):6495-513.
- Vogler EA, Siedlecki CA. Contact activation of blood-plasma coagulation. Biomaterials 2009 Apr;30(10):1857-69.
- Leibner ES, Barnthip N, Chen W, Baumrucker CR, Badding JV, Pishko M, Vogler EA. Superhydrophobic effect on the adsorption of human serum albumin. Acta Biomater 2009 Jun;5(5):1389-98.
- Barnthip N, Noh H, Leibner E, Vogler EA. Volumetric interpretation of protein adsorption: kinetic consequences of a slowly-concentrating interphase. Biomaterials 2008 Jul;29(21):3062-74.
- Noh H, Yohe ST, Vogler EA. Volumetric interpretation of protein adsorption: ion-exchange adsorbent capacity, protein pI, and interaction energetics. Biomaterials 2008 May;29(13):2033-48.
- Zhuo R, Siedlecki CA, Vogler EA. Competitive-protein adsorption in contact activation of blood factor XII. Biomaterials 2007 Oct;28(30):4355-69.
- Noh H, Vogler EA. Volumetric interpretation of protein adsorption: competition from mixtures and the Vroman effect. Biomaterials 2007 Jan;28(3):405-22.
- Krishnan A, Liu YH, Cha P, Allara D, Vogler EA. Interfacial energetics of globular-blood protein adsorption to a hydrophobic interface from aqueous-buffer solution. J R Soc Interface 2006 Apr 22;3(7):283-301.
- Pan Z, Trusler JPM, Jin Z, Zhang K. Interfacial property determination from dynamic pendant-drop characterizations. Nat Protoc 2025 Feb;20(2):363-386.
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