Excipients are added to biopharmaceutical formulations to enhance protein stability and enable the development of robust formulations with acceptable physicochemical properties, but the mechanism by which they confer stability is not fully understood. Here, we aimed to elucidate the mechanism through direct experimental evidence of the binding affinity of an excipient to a monoclonal antibody (mAb), using saturation transfer difference (STD) nuclear magnetic resonance (NMR) spectroscopic method....
[NMR paper] Investigating protein-excipient interactions of a multivalent VHH therapeutic protein using NMR spectroscopy
Investigating protein-excipient interactions of a multivalent VHH therapeutic protein using NMR spectroscopy
Fab Fragment antigen-binding; Fc Fragment crystallizable; HMW High molecular weight; ?HMW Difference between HMW species at stress temperature and 5°C controls; IgG Immunoglobulin G; mAbs Monoclonal antibodies; MV-V(HH) Multivalent V(HH) molecule with the format aC-L(1)-aC-L(1)-aD; NMR Nuclear magnetic resonance; scFv Single-chain fragment variable; SEC Size-exclusion chromatography; V(HH) Variable domain of Heavy chain of Heavy chain-only antibody.
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09-28-2022 06:29 AM
[NMR paper] Convergent Views on Disordered Protein Dynamics From NMR and Computational Approaches
Convergent Views on Disordered Protein Dynamics From NMR and Computational Approaches
Intrinsically disordered proteins (IDPs) or intrinsically disordered regions (IDR) is a class of biologically important proteins exhibiting specific biophysical characteristics. They lack a hydrophobic core and their conformational behavior is strongly influenced by electrostatic interactions. IDPs and IDRs are highly dynamic and a characterization of the motions of IDPs and IDRs is essential for their physically correct description. Nuclear magnetic resonance (NMR) together with molecular...
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09-23-2022 06:24 AM
[NMR paper] Comprehensive Assessment of Protein and Excipient Stability in Biopharmaceutical Formulations Using (1)H NMR Spectroscopy
Comprehensive Assessment of Protein and Excipient Stability in Biopharmaceutical Formulations Using (1)H NMR Spectroscopy
Biopharmaceutical proteins are important drug therapies in the treatment of a range of diseases. Proteins, such as antibodies (Abs) and peptides, are prone to chemical and physical degradation, particularly at the high concentrations currently sought for subcutaneous injections, and so formulation conditions, including buffers and excipients, must be optimized to minimize such instabilities. Therefore, both the protein and small molecule content of biopharmaceutical...
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03-04-2021 12:41 PM
[NMR paper] Deciphering the structural attributes of protein-heparan sulfate interactions using chemo-enzymatic approaches and NMR spectroscopy.
Deciphering the structural attributes of protein-heparan sulfate interactions using chemo-enzymatic approaches and NMR spectroscopy.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/https:--academic.oup.com-images-oup_pubmed.png Related Articles Deciphering the structural attributes of protein-heparan sulfate interactions using chemo-enzymatic approaches and NMR spectroscopy.
Glycobiology. 2021 Feb 06;:
Authors: Préchoux A, Simorre JP, Lortat-Jacob H, Laguri C
Abstract
Heparan sulfates (HS) is a polysaccharide...
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02-15-2021 01:33 PM
[NMR paper] Protein-excipient interactions evaluated via NMR studies in polysorbate based multi-dose protein formulations: influence on antimicrobial efficacy and potential study approach.
Protein-excipient interactions evaluated via NMR studies in polysorbate based multi-dose protein formulations: influence on antimicrobial efficacy and potential study approach.
Related Articles Protein-excipient interactions evaluated via NMR studies in polysorbate based multi-dose protein formulations: influence on antimicrobial efficacy and potential study approach.
J Pharm Sci. 2018 Jun 05;:
Authors: Torosantucci R, Furtmann B, Elshorst B, Pfeiffer-Marek S, Hartleb T, Andres N, Bussemer T
Abstract
Preservatives are excipients...
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06-10-2018 03:09 AM
Protein-excipient interactions evaluated via NMR studies in polysorbate based multi-dose protein formulations: influence on antimicrobial efficacy and potential study approach
Protein-excipient interactions evaluated via NMR studies in polysorbate based multi-dose protein formulations: influence on antimicrobial efficacy and potential study approach
Publication date: Available online 5 June 2018
Source:Journal of Pharmaceutical Sciences</br>
Author(s): Riccardo Torosantucci, Britta Furtmann, Bettina Elshorst, Stefania Pfeiffer-Marek, Tanja Hartleb, Nikolaus Andres, Till Bussemer</br>
Preservatives are excipients essentially needed in pharmaceutical multi-dose formulations to prevent microbial growth. Among available...
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06-06-2018 01:40 AM
Optimal sample formulations for DNP SENS: The importance of radical-surface interactions #DNPNMR
From The DNP-NMR Blog:
Optimal sample formulations for DNP SENS: The importance of radical-surface interactions #DNPNMR
Perras, F.A., et al., Optimal sample formulations for DNP SENS: The importance of radical-surface interactions. Current Opinion in Colloid & Interface Science, 2018. 33: p. 9-18.
http://www.sciencedirect.com/science/article/pii/S1359029417300894
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02-23-2018 07:13 PM
[NMR paper] Ranking high affinity ligands of low solubility by NMR spectroscopy.
Ranking high affinity ligands of low solubility by NMR spectroscopy.
Related Articles Ranking high affinity ligands of low solubility by NMR spectroscopy.
ACS Med Chem Lett. 2011 Jun 9;2(6):485-7
Authors: Landrieu I, Hanoulle X, Fritzinger B, Horvath D, Wieruszeski JM, Lippens G
Abstract
Cyclosporine A (CsA) and its chemical analogues EthVal4Cs, MeVal4Cs, and Me(d-Ala)3EthVal4Cs (Alisporivir) all interact with cyclophilin A (CypA). The latter Alisporivir is a nonimmunosuppressive CsA derivative that has potent anti-HCV properties...
Ranking mAb-excipient interactions in biologics formulations by NMR spectroscopy and computational approaches
Linear Mode
