Temperature and pH dependence of immunoglobulin G conformation

Calmettes, P.; Cser, L.; Rajnavölgyi, Éva

doi:10.1016/0003-9861(91)90135-6

Cited by 44 publications

(32 citation statements)

References 19 publications

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“…The use of three NaCl concentrations examined potential electrostatic effects on the IgG1 structure, whereas heavy water is a known promoter of protein self-association. By comparison, earlier scattering studies on human IgG1 reported few scattering and ultracentrifugation runs or were performed in nonphysiological buffer conditions (28,38,39,(47)(48)(49). Both IgG1 6a and IgG1 19a showed similar experimental R g and R xs values and the same overall length of 16 nm ( Table 1 6.3-6.4 S, which were indistinguishable within error.…”

Section: Discussionmentioning

confidence: 74%

The Solution Structures of Two Human IgG1 Antibodies Show Conformational Stability and Accommodate Their C1q and FcγR Ligands

Rayner

Hui

Gor

et al. 2015

Journal of Biological Chemistry

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Background:The human IgG1 antibody subclass is the most abundant one and is widely used in therapeutic applications. Results: Ultracentrifugation and x-ray/neutron scattering, together with atomistic modeling, revealed asymmetric concentration-independent IgG1 solution structures. Conclusion:The complement and receptor Fc binding sites are not hindered by the Fab regions, explaining its full activity. Significance: These solution structures clarify IgG1 activity and its therapeutic applications.

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Section: Discussionmentioning

confidence: 74%

The Solution Structures of Two Human IgG1 Antibodies Show Conformational Stability and Accommodate Their C1q and FcγR Ligands

Rayner

Hui

Gor

et al. 2015

Journal of Biological Chemistry

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“…The enrichment of immunoglobulin is rather complex due to the fact that the current production techniques result in complex mixtures with a large number of contaminants present [CALMETTES, et al 1991, GALFRE and SECHER 1990, LIU, et al 2002, VANCAN, et al 2002. This section describes the traditional methods available for the enrichment of immunoglobulin.…”

Section: Traditional Methods For Immunoglobulin Enrichmentmentioning

confidence: 99%

Enrichment behavior of immunoglobulin by foam fractionation using response surface methodology

Chen

Parlar

2013

Separation and Purification Technology

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“…This is lower than the 3.86 pKa of lactic acid and the isoelectric point for sheep IgG (5-7.2) [132,133]. In addition, it was reported that fragments of IgG are unstable at a pH less than 5.1 [134]. All of these factors could play a role in why IgG was not measured.…”

Section: Discussionmentioning

confidence: 93%

Drug encapsulated aerosolized microspheres as a biodegradable, intelligent glioma therapy

Floyd

Galperin

Ratner

2015

J Biomedical Materials Res

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Departments of Bioengineering and Chemical EngineeringThe grim prognosis for patients diagnosed with malignant gliomas necessitates the development of new therapeutic strategies for localized and sustained drug delivery to combat tumor drug resistance and regrowth. Here we introduced the novel formulation of drug encapsulated aerosolized microspheres as a biodegradable, intelligent glioma therapy (DREAM BIG Therapy) that is applied post-resection. DREAM BIG Therapy consists of three types of microspheres [poly(lactic acid) (PLA), poly(lactic-co-glycolic acid) (PLGA), and poly(ε-caprolactone) (PCL)] containing various encapsulated chemotherapeutics, suspended in a degradable, aqueous poly(Nisopropylacrylamide) (PNIPAM) solution. The thermoresponsive PNIPAM solution is capable of suspending drug encapsulated microspheres at room temperature which can be "sprayed on" the post-surgical site. The physiological temperature of the treatment site (37°C) would cause PNIPAM solution to solidify and form an adherent gel layer with entrapped microspheres, providing intimate contact with remaining tumor cells. Over time, PLGA (rapid degradation), PLA (medium speed degradation), and then PCL (slow degradation) microspheres would break iv down, releasing their drug payloads in a sequential, multi-drug release directly to the tumor site, addressing cancerous regrowth and tumor drug resistance. This dissertation will address the development of DREAM BIG Therapy, from microsphere formulation to pilot in vivo studies.Initial work focused on developing blank and drug encapsulated microspheres using emulsion techniques. Preliminary studies utilized rhodamine B as a model drug for encapsulation in PLGA, PLA, and PCL particles and optimized formulation parameters to achieve a high encapsulation. Then, gefitinib, IgG, and lomustine were encapsulated in PLGA, PLA, and PCL microspheres, respectively, achieving encapsulation efficiencies greater than 80% and drug loadings greater than 0.3%. The in vitro release of gefitinib and IgG were also studied. Gefitinib released from PLGA microspheres over 40 days while the release of IgG from PLA microspheres was slower, over a year long period.The microsphere-PNIPAM system was tested for aerosolized application ex vivo. The aqueous PNIPAM solution suspended the microspheres and was aerosolized before phase transitioning to an adherent gel layer on the tissue, entrapping the microspheres on the tissue surface. Finally, when tested in vivo, the gefitinib encapsulated PLGA microspheres entrapped in PNIPAM slowed the tumor volume growth of a subcutaneous C6 glioma in comparison to blank PLGA microspheres entrapped in PNIPAM. Overall, this research confirms the potential of DREAM BIG therapy for future use with multiple chemotherapeutics and microsphere types to combat gliomas at a localized site.v

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Temperature and pH dependence of immunoglobulin G conformation

Cited by 44 publications

References 19 publications

The Solution Structures of Two Human IgG1 Antibodies Show Conformational Stability and Accommodate Their C1q and FcγR Ligands

The Solution Structures of Two Human IgG1 Antibodies Show Conformational Stability and Accommodate Their C1q and FcγR Ligands

Enrichment behavior of immunoglobulin by foam fractionation using response surface methodology

Drug encapsulated aerosolized microspheres as a biodegradable, intelligent glioma therapy

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