Zobrazeno 1 - 5
of 5
pro vyhledávání: '"Logan R. Wilks"'
Publikováno v:
ACS Infectious Diseases. 8:2389-2395
An improved method for the generation of peptide vaccines using di-tyrosine cross-linking is described. The conserved ion channel peptide, M2e, of influenza A virus was modified with the addition of small tyrosine-rich regions (GYGY-) at both the N-
Autor:
Tony Y. Shay, Carl A. Karouta, Ayush Sharma, Amjad Chowdhury, Jessica J. Hung, Keith P. Johnston, Maria P. Nieto, Kishan Ramachandran, Logan R. Wilks, Barton J. Dear, Thomas M. Truskett, Jason K. Cheung
Publikováno v:
Industrial & Engineering Chemistry Research. 58:22456-22471
To understand and predict the viscosities of highly concentrated monoclonal antibody (mAb) solutions, it is important to characterize the protein–protein interactions (PPI) and how they influence t...
Autor:
Logan R. Wilks, Joshua R. Laber, Keith P. Johnston, Jessica J. Hung, Thomas M. Truskett, Barton J. Dear, Ayush Sharma
Publikováno v:
Journal of Pharmaceutical Sciences. 108:2517-2526
An understanding of how cosolutes affect the viscosity and storage stability of highly concentrated mAbs as a function of protein-protein interactions (PPIs) would be desirable for improving processing and administration of protein therapeutics. The
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
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