Langmuir-Blodgett films of immunoglobulin G for immunosensors

Turko, Illarion V.; Yurkevich, Igor S.; Chashchin, Vadim L.

doi:10.1016/0040-6090(91)90481-c

Cited by 42 publications

(21 citation statements)

References 6 publications

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“…Different approaches are taken in the self‐assembly of molecules into films and related structures. Examples include Langmuir−Blodgett deposition (6, 7), sol−gel entrapment (8), covalent binding (9), spontaneous adsorption from solution (10, 11), and polyelectrolyte (PE) LbL. The last of these is attractive to biotechnology for several reasons.…”

Section: Introductionmentioning

confidence: 99%

Fine Tuning of Physical Properties of Designed Polypeptide Multilayer Films by Control of pH

Haynie

2006

Biotechnol. Prog.

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Adjustment of pH can alter the ensemble of three-dimensional structures of a polypeptide in solution by changing the distribution of charge and Coulombic interactions. The role of pH in layer-by-layer self-assembly (LbL) of designed 32mer peptides containing the amino acid cysteine has been investigated using a combination of physical methods. Results show that pH can have a substantial influence on the mass of adsorbed peptide, surface roughness, and film density over a range of 1.5 pH units. Peptide film thickness depends on the number of layers, as with "conventional" polyelectrolytes. Film density and morphology, however, vary more with pH than does thickness, translating into a change in density on the order of 70% over the pH range 7.4-8.9. Results of this work provide insight on the physical basis of LbL and suggest that peptides are a promising class of polyelectrolytes for the creation of designer thin films for applications in biotechnology and other areas.

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Section: Introductionmentioning

confidence: 99%

Fine Tuning of Physical Properties of Designed Polypeptide Multilayer Films by Control of pH

Haynie

2006

Biotechnol. Prog.

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“…The LB technique has been used for obtaining monomolecular protein layers on solid surfaces. [1][2][3][4] The spontaneous adsorption of charged proteins onto solid surfaces of opposite charge (e.g. mica) is a widely used technique and also produces monomolecular protein layers.…”

Section: Introductionmentioning

confidence: 99%

2. Assembly of Alternating Polyelectrolyte and Protein Multilayer Films for Immunosensing

et al. 1997

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Alternating polyelectrolyte films constructed by the sequential adsorption of poly(allylamine hydrochloride) (PAH) and poly(styrenesulfonate) (PSS) have been used as substrates for the immobilization of immunoglobulin G (IgG) and anti-IgG. Anti-IgG has also been immobilized in multilayer films by the alternate deposition of PSS and anti-IgG. The assembly process of the multilayer films was monitored using a quartz crystal microbalance (QCM) and surface plasmon resonance (SPR). Film growth was achieved up to at least nine (5 anti-IgG and 4 PSS) layers. The utility of these films for immunosensing has been investigated via their subsequent interaction with IgG. The alternating polyelectrolyte/protein layers were constructed in order to increase the binding layer capacity (i.e. sensitivity) of the thin film with respect to IgG detection. The sensitivity, determined using IgG mass uptake data from quartz crystal microgravimetry, was found to be linearly dependent on the number of anti-IgG layers (and hence the amount of IgG incorporated) in the polyelectrolyte film when the anti-IgG layers are separated by one PSS layer. In contrast, for films where anti-IgG layers are separated by five polyelectrolyte (PSS(PAH/PSS) 2) layers, only the outer anti-IgG layer is immunologically active. This is attributed to the formation of a dense polyelectrolyte film through which antibody permeation is restricted. The films evaluated have promise in that the sensitivity can be tuned by fabricating the desired number of protein layers, whilst the selectivity can be modified by selecting the desired biospecific biomolecule.

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“…Protein films are rapidly becoming a part of this active sphere of research for producing ordered layers of molecules, chiefly because of their potential applications to sensing systems. In particular, IgG (immunoglobulin G) films, which can be employed in immunosensors, have been the object of investigation with attention being paid mainly to their antigen recognition properties. , In spite of the seminal works of authors such as Graham and Phillips and MacRitchie and the more recent efforts made to organize protein monolayers into two-dimensional domain structures, , there remains a large gap in our knowledge of the behavior and characteristics of protein monolayers . In an effort to improve our understanding of the physical processes underlying interfacial phenomena, we have attempted to characterize the mechanical behavior of protein films at the gas−water interface.…”

Section: Introductionmentioning

confidence: 99%

Mechanical Properties of Immunoglobulin G and Albumin Monolayers

1996

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The mechanical properties of protein films at the gas-water interface are determined by means of a mobile barrier. The films are subjected to extensional and compressional surface stresses and strains as opposed to the commonly used shear ones. Two proteins, immunoglobulin G and albumin, with distinctly different characteristics at the interface are investigated. The results from albumin films demonstrate the validity of this method and indicate that, in certain cases, only one measurement is required to completely characterize the elastic constants of the monolayer. From the viscoelastic properties observed for IgG between surface pressures of 3.5 and 26 mN/m, possible mechanisms to explain the film's behavior have been deduced.

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Langmuir-Blodgett films of immunoglobulin G for immunosensors

Cited by 42 publications

References 6 publications

Fine Tuning of Physical Properties of Designed Polypeptide Multilayer Films by Control of pH

Fine Tuning of Physical Properties of Designed Polypeptide Multilayer Films by Control of pH

2. Assembly of Alternating Polyelectrolyte and Protein Multilayer Films for Immunosensing

Mechanical Properties of Immunoglobulin G and Albumin Monolayers

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