Spread Films of Human Serum Albumin at the Air–Water Interface: Optimization, Morphology, and Durability

Campbell, Richard A.; Ang, Joo Chuan; Sebastiani, Federica; Tummino, Andrea; White, John W.

doi:10.1021/acs.langmuir.5b03349

Cited by 19 publications

(33 citation statements)

References 58 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…These fluctuations exceed the error limits and indicated the macroheterogeneity of the layer and the mobility of polydopamine domains. Similar fluctuations have been noted previously for adsorbed layers of human serum albumin [37]. It is possible to assume that the some loose domains of polydopamine are formed at the interface at low concentrations.…”

Section:    supporting

confidence: 84%

See 1 more Smart Citation

Polydopamine layer formation at the liquid – gas interface

Milyaeva

Bykov

Campbell

et al. 2019

Colloids and Surfaces A: Physicochemical and Engineering Aspect

View full text Add to dashboard Cite

The surface properties of a polydopamine layer at the air-water interface were studied by dilatational surface rheology, ellipsometry and Brewster angle microscopy (BAM). A significant increase of the dynamic surface elasticity was discovered when the concentration changed from 0.75 g/l to 2 g/l with the maximum value of about 60 mN/m at a concentration of 1 g/l. The obtained results indicate that the surface film consists of separate domains and the high surface elasticity is a consequence of the interactions between relatively rigid domains of the polymer film. This conclusion was confirmed by Brewster angle microscopy, which demonstrated different steps of the polydopamine film growth. Separate domains appeared at the first step while one can observe a continuous film close to equilibrium. An increase of the initial concentration led to faster polymerization and to the formation of a thicker film. The dynamic surface elasticity decreased in the concentration range from 2 g/l to 5 g/l when the thickness of the polymer film reached about 80 nm. In this case the film could be destroyed in the course of deformation. The cracks in the film resulted in a decrease of the dynamic surface elasticity.

show abstract

Section:    supporting

confidence: 84%

“…Second, ellipsometry can give information about the adsorption extent and kinetics of formation of surface films [34,35]. Lastly, Brewster angle microscopy can give information about the lateral heterogenties present in surface films [36,37].…”

Section: Introductionmentioning

confidence: 99%

Polydopamine layer formation at the liquid – gas interface

Milyaeva

Bykov

Campbell

et al. 2019

Colloids and Surfaces A: Physicochemical and Engineering Aspect

View full text Add to dashboard Cite

show abstract

“…(b), where the isotherm is expanded for the 1 mg mL −1 FN solution as compared with the 0.5 mg mL −1 FN solution. This effect is caused by the Marangoni effect described in detail for bovine serum albumin . If the protein concentration is sufficient, due to spreading from the bulk of the droplets, then protein films can be formed.…”

Section: Resultsmentioning

confidence: 99%

“…This effect is caused by the Marangoni effect described in detail for bovine serum albumin. [17] If the protein concentration is sufficient, due to spreading from the bulk of the droplets, then protein films can be formed. In the case of diluted protein solutions spreading, dissolution of the protein to the subphase dominates and only a textured adsorbed layer forms over time.…”

Section: Resultsmentioning

confidence: 99%

Langmuir–Schaefer films of fibronectin as designed biointerfaces for culturing stem cells

Bhuvanesh

Saretia

Roch

et al. 2016

Polymers for Advanced Techs

View full text Add to dashboard Cite

Glycoproteins adsorbing on an implant upon contact with body fluids can affect the biological response in vitro and in vivo, depending on the type and conformation of the adsorbed biomacromolecules. However, this process is poorly characterized and so far not controllable. Here, protein monolayers of high molecular cohesion with defined density are transferred onto polymeric substrates by the Langmuir–Schaefer (LS) technique and were compared with solution deposition (SO) method. It is hypothesized that on polydimethylsiloxane (PDMS), a substrate with poor cell adhesion capacity, the fibronectin (FN) layers generated by the LS and SO methods will differ in their organization, subsequently facilitating differential stem cell adhesion behavior. Indeed, atomic force microscopy visualization and immunofluorescence images indicated that organization of the FN layer immobilized on PDMS was uniform and homogeneous. In contrast, FN deposited by SO method was rather heterogeneous with appearance of structures resembling protein aggregates. Human mesenchymal stem cells showed reduced absolute numbers of adherent cells, and the vinculin expression seemed to be higher and more homogenously distributed after seeding on PDMS equipped with FN by LS in comparison with PDMS equipped with FN by SO. These divergent responses could be attributed to differences in the availability of adhesion molecule ligands such as the Arg‐Gly‐Asp (RGD) peptide sequence presented at the interface. The LS method allows to control the protein layer characteristics, including the thickness and the protein orientation or conformation, which can be harnessed to direct stem cell responses to defined outcomes, including migration and differentiation. Copyright © 2016 John Wiley & Sons, Ltd.

show abstract

“…We thank the Institut Laue-Langevin (Grenoble, France) for an allocation of neutron beam time on FIGARO (DOI: 10.5291/ILL-DATA.9-12-462), the Partnership for Soft Condensed Matter for access to ancillary equipment, and Peter Wierenga, Emanuel Schneck and Ernesto Scoppola for helpful discussions. We acknowledge the platforms of the Grenoble Instruct-ERIC Center (ISBG: UMS 3518 CNRS-CEA-UGA-EMBL) with support from FRISBI (ANR-10-INSB-05-02) and GRAL (ANR-10-LABX- 49…”

Section: Acknowledgmentsmentioning

confidence: 99%

Adsorption of Denaturated Lysozyme at the Air–Water Interface: Structure and Morphology

et al. 2018

Self Cite

View full text Add to dashboard Cite

The application of protein deuteration and high flux neutron reflectometry has allowed a comparison of the adsorption properties of lysozyme at the air-water interface from dilute solutions in the absence and presence of high concentrations of two strong denaturants: urea and guanidine hydrochloride (GuHCl). The surface excess and adsorption layer thickness were resolved and complemented by images of the mesoscopic lateral morphology from Brewster angle microscopy. It was revealed that the thickness of the adsorption layer in the absence of added denaturants is less than the short axial length of the lysozyme molecule, which indicates deformation of the globules at the interface. Two-dimensional elongated aggregates in the surface layer merge over time to form an extensive network at the approach to steady state. Addition of denaturants in the bulk results in an acceleration of adsorption and an increase of the adsorption layer thickness. These results are attributed to incomplete collapse of the globules in the bulk from the effects of the denaturants as a result of interactions between remote amino acid residues. Both effects may be connected to an increase of the effective total volume of macromolecules due to the changes of their tertiary structure, that is, the formation of molten globules under the influence of urea and the partial unfolding of globules under the influence of GuHCl. In the former case, the increase of globule hydrophobicity leads to cooperative aggregation in the surface layer during adsorption. Unlike in the case of solutions without denaturants, the surface aggregates are short and wormlike, their size does not change with time, and they do not merge to form an extensive network at the approach to steady state. To the best of our knowledge, these are the first observations of cooperative aggregation in lysozyme adsorption layers.

show abstract

Spread Films of Human Serum Albumin at the Air–Water Interface: Optimization, Morphology, and Durability

Cited by 19 publications

References 58 publications

Polydopamine layer formation at the liquid – gas interface

Polydopamine layer formation at the liquid – gas interface

Langmuir–Schaefer films of fibronectin as designed biointerfaces for culturing stem cells

Adsorption of Denaturated Lysozyme at the Air–Water Interface: Structure and Morphology

Contact Info

Product

Resources

About