Rheological study of albumin and hyaluronan-albumin hydrogels: Effect of concentration, ionic strength, pH and molecular weight

Hájovská, Pavla; Chytil, Martin; Kalina, Michal

doi:10.1016/j.ijbiomac.2020.06.063

Cited by 23 publications

(13 citation statements)

References 42 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…As a result, the OA synovial fluid reveals much worse tribological properties. It was shown that increasing the HA concentration results in the gel point shift towards lower temperatures [59] in HAS-HA solutions. Based on this, binding between HA and HSA in OA synovial fluid will decrease (regardless of the increase in calcium ion concentration), and as a result, the complex will not be as stable, which can lead to poor lubrication as it will be diluted with water and ratios between components will change.…”

Section: Resultsmentioning

confidence: 99%

Albumin–Hyaluronan Interactions: Influence of Ionic Composition Probed by Molecular Dynamics

Bełdowski

Przybyłek

Raczyński

et al. 2021

IJMS

View full text Add to dashboard Cite

The lubrication mechanism in synovial fluid and joints is not yet fully understood. Nevertheless, intermolecular interactions between various neutral and ionic species including large macromolecular systems and simple inorganic ions are the key to understanding the excellent lubrication performance. An important tool for characterizing the intermolecular forces and their structural consequences is molecular dynamics. Albumin is one of the major components in synovial fluid. Its electrostatic properties, including the ability to form molecular complexes, are closely related to pH, solvation, and the presence of ions. In the context of synovial fluid, it is relevant to describe the possible interactions between albumin and hyaluronate, taking into account solution composition effects. In this study, the influence of Na+, Mg2+, and Ca2+ ions on human serum albumin–hyaluronan interactions were examined using molecular dynamics tools. It was established that the presence of divalent cations, and especially Ca2+, contributes mostly to the increase of the affinity between hyaluronan and albumin, which is associated with charge compensation in negatively charged hyaluronan and albumin. Furthermore, the most probable binding sites were structurally and energetically characterized. The indicated moieties exhibit a locally positive charge which enables hyaluronate binding (direct and water mediated).

show abstract

Section: Resultsmentioning

confidence: 99%

Albumin–Hyaluronan Interactions: Influence of Ionic Composition Probed by Molecular Dynamics

Bełdowski

Przybyłek

Raczyński

et al. 2021

IJMS

View full text Add to dashboard Cite

show abstract

“…The gel critical temperature of ε-PL-whey protein complexes decreased from 85.5°C to 65.2°C as the pH value increased from 7 to 9. Under alkaline conditions, there was an electrostatic interaction between positively charged ε-PL and negatively charged whey protein (Hájovská et al, 2020). This electrostatic interaction made it easier for the complexes to form gels.…”

Section: Gel Temperature Analysis Of Whey Protein-ε-pl Complexesmentioning

confidence: 99%

“…The critical gel temperature of ε-PL-whey protein complexes decreased with the increase of sodium ion concentration (Figure 6D). It is possible that sodium ions can shield the repulsive force between polymer chains (Hájovská et al, 2020). Sodium ions led to closer binding of the complexes and strengthened the interaction between ε-PL and whey protein.…”

Section: Gel Temperature Analysis Of Whey Protein-ε-pl Complexesmentioning

confidence: 99%

“…The experimental results of Figure 7A4 and Figure 7B4 showed that the concentration of sodium ion could significantly increase the hardness and gumminess of ε-PL-whey protein complex gels (P < 0.01), but there was no significant change in springiness and cohesiveness. Because sodium ion could shield the repulsive force between polymer chains (Hájovská et al, 2020), it leads to the formation of aggregates and strengthens the interaction between ε-PL and whey protein. Thus, it increased the gel hardness and gumminess of the complex gels.…”

Section: Analysis Of Gel Texture Properties Of ε-Pl-whey Protein Comp...mentioning

confidence: 99%

See 1 more Smart Citation

Structure, stability, rheology, and texture properties of ε-polylysine-whey protein complexes

Meng

Xue

Chen

et al. 2022

Journal of Dairy Science

View full text Add to dashboard Cite

ε-Polylysine (ε-PL) is a natural preservative of antimicrobial peptides with broad spectrum and high antibacterial properties. The electrostatic complex delivery system formed by ε-PL and whey protein can be used to maintain the stability of ε-PL and solve the problem of limited application of protein-based food. This work aimed to study the interaction between ε-PL and whey protein by multiple characterization methods. The spectroscopy results showed static quenching type and new stretching of C=O for ε-PL-whey protein complexes. Microstructure studies showed that the combination of ε-PL and whey protein made the structure of the complexes become rough and dense. The interaction between ε-PL and whey protein could improve the stability of the complexes system during storage. Additionally, the interaction affected critical gel temperatures and gel texture properties of complexes with change of whey protein concentration, mass ratio of ε-PL to whey protein, pH value in alkaline solutions, and ion concentration. Overall, this study confirmed the interaction between ε-PL and whey protein, and it will provide a reference for the application of ε-PL in protein food matrix.

show abstract

“…Albumin-based sponge scaffolds/hydrogels can be formed by thermal curing gelation, 9 the redox−oxidation reaction, 10 or addition of external cross-linkers to albumin molecules in solutions, 11−19 and they can be used in bone tissue engineering. With thermal heating of the albumin solution to 60−70 °C, the gelation of albumin hydrogels can be observed by the denaturation of the globular protein and an increase in the intermolecular noncovalent interactions.…”

Section: Introductionmentioning

confidence: 99%

Dynamically and Spatially Controllable Albumin-Based Hydrogels for the Prevention of Postoperative Adhesion

Mao

Peng

Wei

et al. 2021

ACS Biomater. Sci. Eng.

View full text Add to dashboard Cite

Since the degree of severity and the geometry of wounds vary, it is necessary to prepare an antiadhesive hydrogel that possesses dynamically controllable material properties, exhibits biodegradability, and possesses drug-releasing properties. Injectable, oxygen peroxide-sensitive, and photo-cross-linkable hydrogels that permit in situ dynamic and spatial control of their physicochemical properties were synthesized for the prevention of postoperative adhesion. Albumin is the most abundant protein in blood serum and serves as a carrier for several molecules that exhibit poor water solubility. It is therefore a suitable biomaterial for the fabrication of hydrogels since it presents a low risk of life-threatening complications and does not require immunosuppressive therapy for preventing graft rejection. The physicochemical properties of this hydrogel can then be spatially postadjusted via transdermal exposure to light to release drugs, depending on what is required for the injury. A significant reduction in postoperative peritoneal adhesion was observed in an animal model involving severe sidewall and bowel abrasions. This study demonstrated that the fabricated dually cross-linked, albumin-based hydrogels have great potential in such applications because they showed a low immune response, easy handling, full wound coverage, and tunable biodegradability. Precise spatial and controllable drug-release profiles may also be achieved via in situ transdermal post-tuning of the biomaterials, depending on the injury.

show abstract

Rheological study of albumin and hyaluronan-albumin hydrogels: Effect of concentration, ionic strength, pH and molecular weight

Cited by 23 publications

References 42 publications

Albumin–Hyaluronan Interactions: Influence of Ionic Composition Probed by Molecular Dynamics

Albumin–Hyaluronan Interactions: Influence of Ionic Composition Probed by Molecular Dynamics

Structure, stability, rheology, and texture properties of ε-polylysine-whey protein complexes

Dynamically and Spatially Controllable Albumin-Based Hydrogels for the Prevention of Postoperative Adhesion

Contact Info

Product

Resources

About