Zobrazeno 1 - 4
of 4
pro vyhledávání: '"Hassan, Shahfar"'
Publikováno v:
The Journal of Physical Chemistry Letters. 13:1366-1372
Electrostatically driven attractions between proteins can result in issues for therapeutic protein formulations such as solubility limits, aggregation, and high solution viscosity. Previous work showed that a model monoclonal antibody displayed large
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::74e00720e27dbd0886d51e70c00bef05
https://doi.org/10.1021/acs.jpclett.1c03669
https://doi.org/10.1021/acs.jpclett.1c03669
Publikováno v:
Molecular pharmaceutics. 19(11)
Static light scattering (SLS) was used to characterize five monoclonal antibodies (MAbs) as a function of total ionic strength (TIS) at pH values between 5.5 and 7.0. Second osmotic virial coefficient (
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::d99029e59a76ae1ab697937b2ffa45a0
https://pubmed.ncbi.nlm.nih.gov/36194430
https://pubmed.ncbi.nlm.nih.gov/36194430
Publikováno v:
The Journal of Physical Chemistry B. 125:3574-3588
A series of coarse-grained models for molecular simulation of proteins are considered, with emphasis on the application of predicting protein-protein self-interactions for monoclonal antibodies (MAbs). As an illustrative example and for quantitative
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7ce30d7362d836c8a70ba1f715b719cc
https://doi.org/10.1021/acs.jpcb.1c01903
https://doi.org/10.1021/acs.jpcb.1c01903
Autor:
Hassan Shahfar, Glenn M. Ferreira, Hasige A. Sathish, Christopher J. Roberts, Richard L. Remmele
Publikováno v:
The journal of physical chemistry. B. 123(50)
Attractive electrostatic protein-protein interactions (PPI) necessarily involve identifying oppositely charged regions of the protein surface that interact favorably. This cannot be done reliably if one only considers a single protein in isolation un
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f98b6a57ba27dc31724273dba553819b
https://pubmed.ncbi.nlm.nih.gov/31739660
https://pubmed.ncbi.nlm.nih.gov/31739660