Dynamics of protein and mixed protein/surfactant adsorption layers at the water/fluid interface

Miller, R.; Fainerman, V. B.; Makievski, A. V.; Krägel, J.; Grigoriev, D. O.; Kazakov, V. N.; Sinyachenko, O.V.

doi:10.1016/s0001-8686(00)00032-4

Cited by 419 publications

(307 citation statements)

References 89 publications

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“…and PAK3 molecules, as has been previously reported for interactions between proteins and surfactants 25,26 . To test this hypothesis, ELP5 and PAK3 solutions were mixed below the T t (4 °C), which resulted in a disordered white viscous aggregate ( Supplementary Fig.…”

Section: Resultssupporting

confidence: 80%

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Co-assembly, spatiotemporal control and morphogenesis of a hybrid protein–peptide system

et al. 2015

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ature uses self-assembly to create a widespread variety of complex structures with elaborate geometries and outstanding properties 1 such as hierarchical order, adaptability, selfhealing and bioactivity. Developing new bioinspired processes based on dynamic self-assembly could facilitate the fabrication of synthetic three-dimensional (3D) materials with enhanced complexity, dynamic properties and functionality 2 . Proteins are particularly attractive building blocks because of their versatility and biofunctionality 3 . Elastin-like polypeptides (ELPs) 4 are recombinant proteins that have generated great interest 5 as a result of their modular structure, bioactivity, ease of design and production, and the possibility to create robust and elastic materials 5,6 . ELPs allow for a tunable molecular design 7 and are based on the tropoelastin recurrent motif Val-Pro-Gly-X-Gly (VPGXG), in which X is any amino acid other than proline 7 . This repeating pentapeptide provides ELPs with a thermoresponsive behaviour. Below a critical transition temperature (T t ), the ELP molecule undergoes a reversible-phase transition wherein the protein is soluble in aqueous solution and becomes highly solvated, surrounded by clatharate-like water structures. Above the T t , the hydrophobic domains dehydrate and the protein chain hydrophobically collapses and aggregates to form a phaseseparated state 8 .The use of natural and synthetic proteins to create functional materials has been hindered by the difficulty in controlling their conformation and nanoscale assembly with the precision required to form macroscopic materials. This limitation has driven the development of simpler and more-predictable peptide-based materials 9,10 . Peptide amphiphiles (PAs), for example, are synthetic molecules that can self-assemble into nanofibres and create functional 3D hydrogels that emulate the fibrous architecture of the extracellular matrix (ECM) 11,12 . Nonetheless, most peptide and/or protein materials are formed through equilibrium-based self-assembly approaches that are capable of generating stable supramolecular structures, but with limited hierarchy and spatiotemporal control, which has hindered their functionality 2 .Novel approaches based on the dynamic self-assembly of inorganic building blocks [13][14][15] , actin self-organization 16 and the combination of top-down processes with peptide self-assembly have been reported recently 17 . In particular, Stupp and co-workers have described a self-assembling membrane system obtained through strong electrostatic interactions between PAs and oppositely charged polysaccharides 18 . However, the possibility to exploit the unique structural and functional properties of proteins to create dynamic hierarchical materials remains an elusive target. In this study, we attempt to overcome this hurdle by using self-assembling peptides to promote protein conformational changes and guide their assembly into complex, yet functional, materials. We report the discovery and development of a protein/peptide system t...

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Section: Resultssupporting

confidence: 80%

“…The ELP molecules at the air-water interface could enhance the membrane adhesion at the point of contact with the interface (Supplementary Fig. 13) 25,26 . Growth of the tubular structures can be triggered simply by displacing the interface.…”

Section: Resultsmentioning

confidence: 99%

Co-assembly, spatiotemporal control and morphogenesis of a hybrid protein–peptide system

et al. 2015

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“…According to some authors, 37 there is a competitive adsorption between the constituent species of mixed soluble protein/non-ionic surfactant systems. DSAP constitutes, however, a peculiar system due to the presence of the GPI anchor, and its solubility in water, as well as its adsorption, depends on the non-ionic surfactant concentration.…”

Section: Elasticity Measurementsmentioning

confidence: 99%

Adsorption kinetics and dilatational rheological studies for the soluble and anchored forms of alkaline phosphatase at the air/water interface

Caseli¹,

Masui²,

Furriel³

et al. 2005

J. Braz. Chem. Soc.

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Este trabalho apresenta aspectos de equilíbrio e dinâmicos da adsorção na interface ar/líquido de duas formas de fosfatase alcalina de placa óssea de ratos: DSAP, solubilizada com tensoativo não-iônico (C 12 E 9 ), contendo uma âncora de glicosilfosfatidilinositol (GPI), e PLSAP, com a porção hidrofóbica da âncora clivada por fosfolipase-C. A tensão superficial dinâmica, γ dyn , e o módulo de elasticidade superficial dilatacional, ε, foram determinados para soluções de PLSAP, DSAP e C 12 E 9 pelo método de oscilação harmônica e análise do formato da gota eixo-simétrica. Cinéticas de adsorção revelaram que DSAP adsorve trinta vezes mais rapidamente que PLSAP, apresentando um mínimo, e, para PLSAP, a tensão superficial cai continuamente. Para o sistema DSAP/C 12 E 9 , ε atinge um máximo na concentração crítica de agregação (CAC), mas para PLSAP, ε diminui continuamente com a concentração. Soluções de C 12 E 9 apresentam ε mais elevados, decrescentes com a concentração. Um modelo, baseado na influência da âncora GPI, é proposto para explicar os resultados obtidos.This work presents equilibrium and dynamic aspects for the adsorption at the air/liquid interface of two rat osseous plate alkaline phosphatase forms: DSAP, solubilized by a surfactant, C 12 E 9 , and containing a glycosylphosphatidylinositol (GPI) anchor; and PLSAP, resulting from phospholipase-C cleavage of the hydrophobic portion of the GPI anchor. Dynamic surface tension, γ dyn , and surface elasticity modulus, ε, were determined for PLSAP, DSAP and pure C 12 E 9 solutions using harmonic oscillation and axisymmetric drop shape analysis Adsorption kinetics studies revealed that DSAP adsorbs thirty times faster than PLSAP, presenting a minimum in the curve. For DSAP/ C 12 E 9 mixed system, ε increases with concentration and a maximum appears at the critical aggregation concentration (CAC). For PLSAP, a continuous decreasing with concentration for γ dyn and ε was observed. For pure C 12 E 9 solution , the elasticity modulus increases with concentration and ε values are higher when compared to the mixed system. A model based on the influence of the GPI anchor is proposed.Keywords: dynamic surface tension, adsorption kinetics, dilatational surface elasticity, alkaline phosphatase, axisymmetric drop shape analysis IntroductionSurface elasticity is associated with the ability of a system to establish a new surface tension value due to a timely area variation. Considering that it is a nonequilibrium phenomenon, changes in surface tension occur either as a consequence of a sudden compression/ expansion of the interface, or due to a local concentration variation. Since elasticity values are associated with diffusion processes, adsorption/desorption, as well as the rearrangement of molecules at the interface, they depend on the time scale (or frequency) in which the perturbation is applied. In addition, these processes are influenced by molecular weight, shape and molecular interactions of the species present at the interface.Surface elasticity is directly relate...

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“…Proteins adsorbed at air-liquid interfaces can expose hydrophobic parts causing partial unfolding or undergo modification in polypeptide conformation. This has already been studied for ␤ casein, bovine serum albumin, lysozyme and ovalbumine [67][68][69]. Ranaldi et al [54] investigated structural changes of HPL in acidic conditions by attenuated total reflectance Fourier transform infrared spectroscopy and electron paramagnetic resonance spectroscopy, and concluded that for pH 6.5-3.0 the secondary structure of HPL is maintained, while at pH below 3.0 HPL is completely unfolded with irreversible loss of the enzymatic activity.…”

Section: Resultsmentioning

confidence: 98%

Chitosan does not inhibit enzymatic action of human pancreatic lipase in Langmuir monolayers of 1,2-didecanoyl-glycerol (DDG)

Souza

Pavinatto

Caseli

et al. 2014

Colloids and Surfaces B: Biointerfaces

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Dynamics of protein and mixed protein/surfactant adsorption layers at the water/fluid interface

Cited by 419 publications

References 89 publications

Co-assembly, spatiotemporal control and morphogenesis of a hybrid protein–peptide system

Co-assembly, spatiotemporal control and morphogenesis of a hybrid protein–peptide system

Adsorption kinetics and dilatational rheological studies for the soluble and anchored forms of alkaline phosphatase at the air/water interface

Chitosan does not inhibit enzymatic action of human pancreatic lipase in Langmuir monolayers of 1,2-didecanoyl-glycerol (DDG)

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