Thermodynamic stability and formation of aggregates of human immunoglobulin G characterised by differential scanning calorimetry and dynamic light scattering

Ahrer, Karin; Buchacher, Andrea; Iberer, Günter; Jungbauer, Alois

doi:10.1016/j.jbbm.2005.12.003

Cited by 78 publications

(48 citation statements)

References 31 publications

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“…3.2.5 Measurement of thermal stability of the MPS-immobilized antibody by DSC 33) In order to confirm the structural stability of the antibody after adsorption on MPS, DSC was performed for both free antibody and MPS-antibody composites (Fig. 11).…”

Section: Acetonitrile Stability and Thermal Stability Of The Mps-immomentioning

confidence: 99%

Immobilization of antibodies on mesoporous silica materials and their binding abilities to antigens

Orita

Kato

Tomita

2011

J. Ceram. Soc. Japan

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Mesoporous silicas (MPS) are potential materials for adsorption of antibodies on their surface as they have the following features: a) an ordered pore network and b) a high surface area. These unique features make MPS an excellent candidate as an immobilizing carrier for immunoassays. We present here the relationship between antibody molecules and pore diameters of various MPS; moreover, the thermal stability and the organic solvent stability of antibodies immobilized on MPS are evaluated. From six MPS, the entire amount of antibodies (44 µg) was adsorbed on four MPS (3 mg; pore sizes: 3.4, 11.0, 15.0, and 23.1 nm) but not on MPS with 5.8 and 8.1 nm pores. However, the binding activities of antibodies to antigens were high only on MPS with 3.4 and 5.8 nm pores. Regarding the thermal stability of antibodies immobilized on MPS, the antibody immobilized on 23.1 nm pore MPS kept about 30% activity even after 3 h at 80°C, but that on 3.4 nm pore MPS was markedly decreased (<10% activity) after that time. These results indicated that the Fab fragment, which is an antigen binding site of the antibody, was incorporated inside larger pores but remained outside smaller pores.

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Section: Acetonitrile Stability and Thermal Stability Of The Mps-immomentioning

confidence: 99%

Immobilization of antibodies on mesoporous silica materials and their binding abilities to antigens

Orita

Kato

Tomita

2011

J. Ceram. Soc. Japan

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“…Process steps in the biotechnological purification sector where knowledge of protein solubility is absolutely crucial comprise controlled protein precipitation and crystallization (Thommes and Etzel, 2007;Low et al, 2007;Cheng et al, 2006), chromatography (Gagnon et al, 1997;To and Lenhoff, 2007;Valente et al, 2006), ATPS (Hachem et al, 1996;Berggren et al, 2002) and protein formulation (Black et al, 2007;Ahrer et al, 2006). When determining solubility data for the development of such processes, one has to distinguish between the requirement of thermodynamically sound data and`rough' estimates on regions where spontaneous precipitation might occur.…”

Section: Introductionmentioning

confidence: 99%

A novel method to evaluate protein solubility using a high throughput screening approach

Wiendahl

Völker

Husemann

et al. 2009

Chemical Engineering Science

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“…Although sensitive to increasing radius of protein gyration during aggregation, DLS can be insensitive to unfolding mechanisms not affecting the size of the protein. In addition to optical techniques, the exo-endothermic probing of differential scanning calorimetry (DSC) has become a key tool to examine a protein's denaturation and glass transition temperature141516. While providing valuable information, all these techniques can generally only thermally probe one sample at a time, which imposes severe limitations on screening studies or for analytical statistics.…”

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confidence: 99%

Differential Scanning Fluorimetry provides high throughput data on silk protein transitions.

Vollrath

Hawkins

Porter

et al. 2014

Sci Rep

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Here we present a set of measurements using Differential Scanning Fluorimetry (DSF) as an inexpensive, high throughput screening method to investigate the folding of silk protein molecules as they abandon their first native melt conformation, dehydrate and denature into their final solid filament conformation. Our first data and analyses comparing silks from spiders, mulberry and wild silkworms as well as reconstituted ‘silk' fibroin show that DSF can provide valuable insights into details of silk denaturation processes that might be active during spinning. We conclude that this technique and technology offers a powerful and novel tool to analyse silk protein transitions in detail by allowing many changes to the silk solutions to be tested rapidly with microliter scale sample sizes. Such transition mechanisms will lead to important generic insights into the folding patterns not only of silks but also of other fibrous protein (bio)polymers.

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Thermodynamic stability and formation of aggregates of human immunoglobulin G characterised by differential scanning calorimetry and dynamic light scattering

Cited by 78 publications

References 31 publications

Immobilization of antibodies on mesoporous silica materials and their binding abilities to antigens

Immobilization of antibodies on mesoporous silica materials and their binding abilities to antigens

A novel method to evaluate protein solubility using a high throughput screening approach

Differential Scanning Fluorimetry provides high throughput data on silk protein transitions.

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