Native-state solubility and transfer free energy as predictive tools for selecting excipients to include in protein formulation development studies

Journal of Pharmaceutical Sciences

Volumn 101, Issue 8, 2012, Pages 2720-2732

  Banks, Douglas D ^a   Latypov, Ramil F ^a   Ketchem, Randal R ^a   Woodard, Jon ^a   Scavezze, Joanna L ^a   Siska, Christine C ^a   Razinkov, Vladimir I ^a  

^a AMGEN INC   (United States)

Author keywords

Aggregation; Conformational stability; Excipient; Kinetics; Monoclonal antibody; Protein formulation; Solubility; Thermodynamics; Transfer free energy

Indexed keywords

AMMONIUM SULFATE; EXCIPIENT; IMMUNOGLOBULIN G1 ANTIBODY; MACROGOL; MONOCLONAL ANTIBODY; WATER;

ARTICLE; CIRCULAR DICHROISM; DIFFERENTIAL SCANNING CALORIMETRY; DRUG FORMULATION; DRUG STABILITY; ENERGY; GEL PERMEATION CHROMATOGRAPHY; KINETICS; MODEL; NONHUMAN; PH; PREDICTION; PROTEIN AGGREGATION; PROTEIN CONFORMATION; PROTEIN STABILITY; SOLUBILITY; THERMODYNAMICS; ULTRAVIOLET SPECTROSCOPY;

EID: 84862876623     PISSN: 00223549     EISSN: 15206017     Source Type: Journal    
DOI: 10.1002/jps.23219     Document Type: Article

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