The effect of solvent environment on the conformation and stability of human polyclonal IgG in solution

Szenczi, Árpád; Kardos, József; Medgyesi, G; Závodszky, Péter

doi:10.1016/j.biologicals.2005.06.007

Cited by 69 publications

(38 citation statements)

References 25 publications

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“…Although hIgG has higher stability at pH 7.0, there is a tendency for aggregation due to the proximity to the isoelectric point. 43 This pattern was also reported in other systems in which the pH was near the isoelectric point of the protein attached to the metal NP. 44 Moreover, the charge distribution of the biomolecules involved is a factor of great influence in the stabilization process.…”

Section: Resultssupporting

confidence: 73%

“…However, this conjugation method proved to be effective when used in the development of immunoassays employing metal nanoparticles, 13 and no aggregation was observed before addition of NaClO4. [42][43][44] Additionally, the effect of anti-hIgG concentration was investigated in the range of 150 and 750 ng mL -1 . The best performance was observed using 150 ng mL -1 anti-hIgG.…”

Section: Resultsmentioning

confidence: 99%

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Immunoassay for Human IgG Using Antibody-functionalized Silver Nanoparticles

2017

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A simple colorimetric immunoassay for quantification of human immunoglobulin G (hIgG) is herein described. The assay is based on the aggregation inhibition of silver nanoparticles (AgNP) functionalized with hIgG antibody (anti-hIgG) on the surface. The aggregation is measured in terms of attenuance values ratio at 400 and 530 nm (A400/A530). A linear response between A400/A530 and hIgG concentration is observed in the range 25 -200 ng mL -1 , and the detection limit is estimated as 11 ng mL -1 hIgG.

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Section: Resultssupporting

confidence: 73%

Section: Resultsmentioning

confidence: 99%

Immunoassay for Human IgG Using Antibody-functionalized Silver Nanoparticles

2017

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“…7 Efforts to reduce aggregation include the addition of polyols, sugars, polymers, amino acids, detergents, and denaturants, which either stabilize the native state or shield the denatured state against intermolecular contacts. [8][9][10][11][12][13] In general, these stabilizers work through weak and nonspecific preferential exclusion, although detergents may work by more specific shielding of hydrophobic patches.…”

Section: Introductionmentioning

confidence: 99%

pH‐dependent aggregation of cutinase is efficiently suppressed by 1,8‐ANS

Pedersen

Nesgaard

Baptista³

et al. 2006

Biopolymers

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We have studied the thermal stability of the triglyceride-hydrolyzing enzyme cutinase from F. solani pisi at pH values straddling the pI (pH 8.0). At the pI, increasing the protein concentration from 5 to 80 microM decreases the apparent melting temperature by 19 degrees C. This effect vanishes at pH values more than one unit away from pI. In contrast to additives such as detergents and osmolytes, the hydrophobic fluorophore 1,8-ANS completely and saturably suppresses this effect, restoring 70% of enzymatic activity upon cooling. ANS binds strongly to native cutinase as a noncompetitive inhibitor with up to 5 ANS per cutinase molecule. Only the first ANS molecule stabilizes cutinase; however, the last 4 ANS molecules decrease Tm by up to 7 degrees C. Similar pI-dependent aggregation and suppression by ANS is observed for T. lanuginosus lipase, but not for lysozyme or porcine alpha-amylase, suggesting that this behavior is most prevalent for proteins with affinity for hydrophobic substrates and consequent exposure of hydrophobic patches. Aggregation may be promoted by a fluctuating ensemble of native-like states associating via intermolecular beta-sheet rich structures unless blocked by ANS. Our data highlight the chaperone activity of small molecules with affinity for hydrophobic surfaces and their potential application as stabilizers at appropriate stoichiometries.

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“…Such an investigation is necessary to determine whether the therapeutic application of IVIg should be preceded by HLA antibody screening. Commercially available IVIg preparations, depending on their polyreactive and their polyclonal antibody strength may contain variable amounts of IgG dimers in the range of 5-15% [36], although IgG dimer, unlike polymers, does not cause anaphylactic shock. Nevertheless IVIg preparations with high dimer content are less tolerated and can give rise to undesirable side effects such as fever, nausea and sometimes lowered blood pressure [37,38].…”

Section: Introductionmentioning

confidence: 99%