The Interaction Between Polysaccharides and Other Macromolecules. 4. The Osmotic Pressure of Mixtures of Serum Albumin and Hyaluronic Acid

Laurent, Torward C.; Ogston, A. G.

doi:10.1042/bj0890249

Cited by 178 publications

(95 citation statements)

References 7 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Laurent and Ogston found that the osmotic pressure of a serum albumin-hyaluronic acid mixture is much higher than the sum of the osmotic pressures of the individual components, suggesting some interaction. 46 The viscosity of hyaluronic acid undergoes a 3-fold increase when it is combined with synovial fluid proteins; since albumin is the most concentrated protein in synovial fluid, this increase in viscosity has been attributed to an expansion of hyaluronic acid upon binding albumin. 47 Rheological changes upon combination of HA with serum albumin have also been noted by Colby and co-workers.…”

Section: Resultsmentioning

confidence: 99%

Identification by Integrated Computer Modeling and Light Scattering Studies of an Electrostatic Serum Albumin-Hyaluronic Acid Binding Site

et al. 2001

View full text Add to dashboard Cite

Dynamic light scattering and turbidimetry, carried out on solutions of hyaluronic acid (HA) and bovine or human serum albumin (SA) at fixed ionic strength (I), revealed a critical pH corresponding to the onset of HA-SA soluble complex formation. Subsequent reduction of pH below pH c , corresponding to an increase in protein net positive charge, results in phase separation of the complex. The sensitivity of pH c to I indicated the primacy of electrostatic interactions in this process. Since pH c was always above the pK a of HA, these effects could be attributed to the influence of protein charge. The electrostatic potential around HSA was modeled using DelPhi (MSI) under pH, I conditions corresponding to incipient binding, phase separation, and noninteraction. At all incipient binding conditions (i.e., pH c , at varying I), an identical region of positive potential 5 Å from the protein van der Waals surface appeared. This unique domain intensified with a decrease in pH or I (corresponding to stronger binding), and diminished with an increase in pH or I (i.e., at noninteracting conditions). The size and low curvature of this domain could readily accommodate a 12 nm (decamer) sequence of HA. Simple electrostatic considerations indicate an electrostatic binding energy for the formation of this complex of ca. 1 kT, consistent with the condition of incipient complex formation. We suggest that such weak electrostatic binding may characterize nonspecific interactions for other proteingylcosaminoglycan pairs.

show abstract

Section: Resultsmentioning

confidence: 99%

Identification by Integrated Computer Modeling and Light Scattering Studies of an Electrostatic Serum Albumin-Hyaluronic Acid Binding Site

et al. 2001

View full text Add to dashboard Cite

show abstract

“…However, the importance of volume exclusion for biomolecules was already recognized by Ogsteen and Laurent in the 1960s from studies of the connective tissue polysaccharide hyaluronan (Laurent and Ogston 1963).…”

Section: Introductionmentioning

confidence: 99%

“…Due to excluded volume effects, any reaction resulting in a volume change will be affected by macromolecular crowding (Laurent and Ogston 1963;Minton 2005). It has been suggested that macromolecular crowding provides a stabilizing effect to the folded states of proteins indirectly due to destabilization of the more extended and malleable denatured states (Zhou 2004;Cheung et al 2005).…”

Section: Introductionmentioning

confidence: 99%

Effects of macromolecular crowding agents on protein folding in vitro and in silico

et al. 2013

View full text Add to dashboard Cite

Proteins fold and function inside cells which are environments very different from that of dilute buffer solutions most often used in traditional experiments. The crowded milieu results in excluded-volume effects, increased bulk viscosity and amplified chances for intermolecular interactions. These environmental factors have not been accounted for in most mechanistic studies of protein folding executed during the last decades. The question thus arises as to how these effects-present when polypeptides normally fold in vivo-modulate protein biophysics. To address excluded volume effects, we use synthetic macromolecular crowding agents, which take up significant volume but do not interact with proteins, in combination with strategically selected proteins and a range of equilibrium and time-resolved biophysical (spectroscopic and computational) methods. In this review, we describe key observations on macromolecular crowding effects on protein stability, folding and structure drawn from combined in vitro and in silico studies. As expected based on Minton's early predictions, many proteins (apoflavodoxin, VlsE, cytochrome c, and S16) became more thermodynamically stable (magnitude depends inversely on protein stability in buffer) and, unexpectedly, for apoflavodoxin and VlsE, the folded states changed both secondary structure content and, for VlsE, overall shape in the presence of macromolecular crowding. For apoflavodoxin and cytochrome c, which have complex kinetic folding mechanisms, excluded volume effects made the folding energy landscapes smoother (i.e., less misfolding and/or kinetic heterogeneity) than in buffer.

show abstract

“…14 Rheological investigations may also provide insight into the near frictionless lubrication of bone articulation, the mechanism of which is not fully understood. 15,16 Scattering measurements have been used to investigate the effect of different counterions on the molecular conformation of HA both in the solid state and in solution. [17][18][19] Anomalous SAXS has revealed changes in the counterion distribution around the HA filaments due to monovalentdivalent ion exchange.…”

Section: Introductionmentioning

confidence: 99%

Ions in hyaluronic acid solutions

Horkay

Basser

Londono

et al. 2009

The Journal of Chemical Physics

View full text Add to dashboard Cite

Hyaluronic acid ͑HA͒ is an anionic biopolymer that is almost ubiquitous in biological tissues. An attempt is made to determine the dominant features that account for both its abundance and its multifunctional role, and which set it apart from other types of biopolymers. A combination of osmotic and scattering techniques is employed to quantify its dynamic and static properties in near-physiological solution conditions, where it is exposed both to mono-and divalent counterions. An equation of state is derived for the osmotic pressure ⌸ in the semidilute concentration region, in terms of two variables, the polymer concentration c and the ionic strength J of the added salt, according to which ⌸ = 1.4ϫ 10 3 c 9/4 / J 3/4 kPa, where c and J are expressed in mole. Over the physiological ion concentration range, the effect of the sodium chloride and calcium chloride on the osmotic properties of HA solutions is fully accounted for by their contributions to the ionic strength. The absence of precipitation, even at high CaCl 2 concentrations, distinguishes this molecule from other biopolymers such as DNA. Dynamic light scattering measurements reveal that the collective diffusion coefficient in HA solutions exceeds that in aqueous solutions of typical neutral polymers by a factor of approximately 5. This property ensures rapid adjustment to, and recovery from, stress applied to HA-containing tissue. Small angle x-ray scattering measurements confirm the absence of appreciable structural reorganization over the observed length scale range 10-1000 Å, as a result of calcium-sodium ion exchange. The scattered intensity in the transfer momentum range q Ͼ 0.03 Å −1 varies as 1 / q, indicating that the HA chain segments in semidilute solutions are linear over an extended concentration range. The osmotic compression modulus c ‫ץ‬ ⌸ / ‫ץ‬c, a high value of which is a prerequisite in structural biopolymers, is several times greater than in typical neutral polymer solutions.

show abstract

The Interaction Between Polysaccharides and Other Macromolecules. 4. The Osmotic Pressure of Mixtures of Serum Albumin and Hyaluronic Acid

Cited by 178 publications

References 7 publications

Identification by Integrated Computer Modeling and Light Scattering Studies of an Electrostatic Serum Albumin-Hyaluronic Acid Binding Site

Identification by Integrated Computer Modeling and Light Scattering Studies of an Electrostatic Serum Albumin-Hyaluronic Acid Binding Site

Effects of macromolecular crowding agents on protein folding in vitro and in silico

Ions in hyaluronic acid solutions

Contact Info

Product

Resources

About