Zobrazeno 1 - 10
of 10
pro vyhledávání: '"P. Douglas Godfrin"'
Publikováno v:
Soft Matter. 14:5604-5614
Many soft matter systems have properties which depend on their processing history. It is generally accepted that material properties can be finely tuned by carefully directing self-assembly. However, for gelling colloidal systems, it is difficult to
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::40a66ba406476243c9b8e483bcce125e
https://doi.org/10.1039/c8sm00814k
https://doi.org/10.1039/c8sm00814k
Autor:
P. Douglas Godfrin, Jessica J. Hung, Tony Y. Shay, Jason K. Cheung, Ayush Sharma, Keith P. Johnston, Maria P. Nieto, Amjad Chowdhury, Thomas M. Truskett, Dmytro Nykypanchuk, Jonathan A. Bollinger, Barton J. Dear, Carl A. Karouta, Kishan Ramachandran, Logan R. Wilks
Publikováno v:
The journal of physical chemistry. B. 123(25)
Attractive protein?protein interactions (PPI) in concentrated monoclonal antibody (mAb) solutions may lead to reversible oligomers (clusters) that impact colloidal stability and viscosity. Herein, the PPI are tuned for two mAbs via the addition of ar
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fb07e838aca0990d52e38a8794c881ed
https://pubmed.ncbi.nlm.nih.gov/31146525
https://pubmed.ncbi.nlm.nih.gov/31146525
Autor:
Jonathan A. Bollinger, Jason K. Cheung, P. Douglas Godfrin, Amjad Chowdhury, Barton J. Dear, Thomas M. Truskett, Ayush Sharma, Jessica J. Hung, Kishan Ramachandran, Keith P. Johnston, Tony Y. Shay, Carl A. Karouta, Maria P. Nieto, Logan R. Wilks
Publikováno v:
The journal of physical chemistry. B. 123(4)
The ability to design and formulate mAbs to minimize attractive interactions at high concentrations is important for protein processing, stability, and administration, particularly in subcutaneous delivery, where high viscosities are often challengin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b2ae31138bd751a62e26da14ac86505d
https://pubmed.ncbi.nlm.nih.gov/30614707
https://pubmed.ncbi.nlm.nih.gov/30614707
Autor:
Abu Zayed Md Badruddoza, P. Douglas Godfrin, Patrick S. Doyle, Allan S. Myerson, Bernhardt L. Trout
Publikováno v:
Advanced Healthcare Materials. 5:1960-1968
Although roughly 40% of pharmaceuticals being developed are poorly water soluble, this class of drugs lacks a formulation strategy capable of producing high loads, fast dissolution kinetics, and low energy input. In this work, a novel bottom-up appro
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0466fa6f5fa1c1ee3242e58f2b6f05a2
https://doi.org/10.1002/adhm.201600266
https://doi.org/10.1002/adhm.201600266
Autor:
P. Douglas Godfrin, Yun Liu, Peter Falus, Jonathan Zarzar, Lionel Porcar, Norman J. Wagner, Isidro E. Zarraga
Publikováno v:
The Journal of Physical Chemistry B. 120:278-291
Recently, reversible cluster formation was identified as an underlying cause of anomalously large solution viscosities observed in some concentrated monoclonal antibody (mAb) formulations, which poses a major challenge to the use of subcutaneous inje
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::45915e2ba1f60070fffa94b6d46e3502
https://doi.org/10.1021/acs.jpcb.5b07260
https://doi.org/10.1021/acs.jpcb.5b07260
Publikováno v:
The journal of chemical physics 148(6), 065101-(2018). doi:10.1063/1.5016517
Recently, atypical static features of microstructural ordering in low-salinity lysozyme protein solutions have been extensively explored experimentally and explained theoretically based on a short-range attractive plus long-range repulsive (SALR) int
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b9bb5d48adbe0b02e6865302a72a3e89
https://pubmed.ncbi.nlm.nih.gov/29448794
https://pubmed.ncbi.nlm.nih.gov/29448794
Autor:
P. Douglas Godfrin, Norman J. Wagner, Steven D. Hudson, Lionel Porcar, Peter Falus, Yun Liu, Kunlun Hong
Publikováno v:
Physical Review Letters. 115
The glass transition of colloidal dispersions interacting with both a short-ranged attraction and long-ranged repulsion is studied using highly purified lysozyme solutions. Newtonian liquid behavior is observed at all conditions while measurements of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::249d8cc3e688481259db8b904ca33339
https://doi.org/10.1103/physrevlett.115.228302
https://doi.org/10.1103/physrevlett.115.228302
Generalized phase behavior of cluster formation in colloidal dispersions with competing interactions
Autor:
Ramón Castañeda-Priego, Yun Liu, Norman J. Wagner, P. Douglas Godfrin, Néstor E. Valadez-Pérez
Publikováno v:
Soft matter. 10(28)
Colloidal liquids interacting with short range attraction and long range repulsion, such as proposed for some protein solutions, have been found to exhibit novel states consisting of equilibrium particle clusters. Monte Carlo simulations are performe
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::90074bbff7e4333b24ce39c15f66e02f
https://pubmed.ncbi.nlm.nih.gov/24899107
https://pubmed.ncbi.nlm.nih.gov/24899107
Autor:
P. Douglas Godfrin, Aaron P. R. Eberle, Norman J. Wagner, Lionel Porcar, Paul Butler, A. Kate Gurnon
A new small-angle neutron scattering (SANS) sample environment optimized for studying the microstructure of complex fluids under simple shear flow is presented. The SANS shear cell consists of a concentric cylinder Couette geometry that is sealed and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::54a92d4616519e508e3bdc99667fe9e0
https://europepmc.org/articles/PMC4116790/
https://europepmc.org/articles/PMC4116790/
Publikováno v:
The Journal of chemical physics. 139(15)
Colloidal dispersions with a short-range attraction and long-range repulsion can exhibit an intriguing intermediate range order, manifested in scattering experiments as a low-q peak in the structure factor. Monte Carlo simulations are performed on fl
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fe08bac6898cde6d086ae9c1d4cb69bd
https://pubmed.ncbi.nlm.nih.gov/24160543
https://pubmed.ncbi.nlm.nih.gov/24160543