Abstract
A principal conclusion drawn from observations of time- and concentration-dependent liquid-vapor (LV) interfacial tension γ lv of a diverse selection of proteins ranging from albumin to ubiquitin spanning nearly three decades in molecular weight (MW) is that concentration scaling substantially alters perception of protein interfacial activity as measured by reduction in γlv. Proteins appear more similar than dissimilar on a weight/volume basis, whereas molarity scaling reveals a "Traube-rule" ordering by MW, suggesting that adsorption is substantially driven by solution concentration rather than diversity in protein amphilicity. Scaling as a ratio-to-physiological-concentration demonstrates that certain proteins exhibit the full possible range of interfacial activity at and well-below physiological concentration, whereas others are only weakly surface active within this range, requiring substantially higher solution concentration to achieve reduction in γlv. Important among this latter category of proteins are the blood factors XII and XIIa, assumed by the classical biochemical mechanism of plasma coagulation to adsorb to procoagulant surfaces, even in the presence of overwhelming concentrations of other blood constituents such as albumin and immunoglobulin that are shown by this work to be among the class of highly surface-active proteins at physiologic concentration. A comparison of pendant drop and Wilhelmy balance tensiometry as tools for assessing protein interfacial activity shows that measurement conditions employed in the typical Wilhelmy plate approach fails to achieve the steady-state adsorption condition that is accessible to pendant drop tensiometry.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 544-557 |
| Number of pages | 14 |
| Journal | Journal of Biomedical Materials Research - Part A |
| Volume | 68 |
| Issue number | 3 |
| DOIs | |
| State | Published - Feb 1 2004 |
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All Science Journal Classification (ASJC) codes
- Ceramics and Composites
- Biomaterials
- Biomedical Engineering
- Metals and Alloys
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Scaled interfacial activity of proteins at the liquid-vapor interface. / Krishnan, Anandi; Sturgeon, Jacqueline; Siedlecki, Christopher A.; Vogler, Erwin A.
In: Journal of Biomedical Materials Research - Part A, Vol. 68, No. 3, 01.02.2004, p. 544-557.Research output: Contribution to journal › Article
TY - JOUR
T1 - Scaled interfacial activity of proteins at the liquid-vapor interface
AU - Krishnan, Anandi
AU - Sturgeon, Jacqueline
AU - Siedlecki, Christopher A.
AU - Vogler, Erwin A.
PY - 2004/2/1
Y1 - 2004/2/1
N2 - A principal conclusion drawn from observations of time- and concentration-dependent liquid-vapor (LV) interfacial tension γ lv of a diverse selection of proteins ranging from albumin to ubiquitin spanning nearly three decades in molecular weight (MW) is that concentration scaling substantially alters perception of protein interfacial activity as measured by reduction in γlv. Proteins appear more similar than dissimilar on a weight/volume basis, whereas molarity scaling reveals a "Traube-rule" ordering by MW, suggesting that adsorption is substantially driven by solution concentration rather than diversity in protein amphilicity. Scaling as a ratio-to-physiological-concentration demonstrates that certain proteins exhibit the full possible range of interfacial activity at and well-below physiological concentration, whereas others are only weakly surface active within this range, requiring substantially higher solution concentration to achieve reduction in γlv. Important among this latter category of proteins are the blood factors XII and XIIa, assumed by the classical biochemical mechanism of plasma coagulation to adsorb to procoagulant surfaces, even in the presence of overwhelming concentrations of other blood constituents such as albumin and immunoglobulin that are shown by this work to be among the class of highly surface-active proteins at physiologic concentration. A comparison of pendant drop and Wilhelmy balance tensiometry as tools for assessing protein interfacial activity shows that measurement conditions employed in the typical Wilhelmy plate approach fails to achieve the steady-state adsorption condition that is accessible to pendant drop tensiometry.
AB - A principal conclusion drawn from observations of time- and concentration-dependent liquid-vapor (LV) interfacial tension γ lv of a diverse selection of proteins ranging from albumin to ubiquitin spanning nearly three decades in molecular weight (MW) is that concentration scaling substantially alters perception of protein interfacial activity as measured by reduction in γlv. Proteins appear more similar than dissimilar on a weight/volume basis, whereas molarity scaling reveals a "Traube-rule" ordering by MW, suggesting that adsorption is substantially driven by solution concentration rather than diversity in protein amphilicity. Scaling as a ratio-to-physiological-concentration demonstrates that certain proteins exhibit the full possible range of interfacial activity at and well-below physiological concentration, whereas others are only weakly surface active within this range, requiring substantially higher solution concentration to achieve reduction in γlv. Important among this latter category of proteins are the blood factors XII and XIIa, assumed by the classical biochemical mechanism of plasma coagulation to adsorb to procoagulant surfaces, even in the presence of overwhelming concentrations of other blood constituents such as albumin and immunoglobulin that are shown by this work to be among the class of highly surface-active proteins at physiologic concentration. A comparison of pendant drop and Wilhelmy balance tensiometry as tools for assessing protein interfacial activity shows that measurement conditions employed in the typical Wilhelmy plate approach fails to achieve the steady-state adsorption condition that is accessible to pendant drop tensiometry.
UR - http://www.scopus.com/inward/record.url?scp=1342322856&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=1342322856&partnerID=8YFLogxK
U2 - 10.1002/jbm.a.20104
DO - 10.1002/jbm.a.20104
M3 - Article
C2 - 14762935
AN - SCOPUS:1342322856
VL - 68
SP - 544
EP - 557
JO - Journal of Biomedical Materials Research - Part A
JF - Journal of Biomedical Materials Research - Part A
SN - 1549-3296
IS - 3
ER -