Significance of unfolding thermodynamics for predicting aggregation kinetics: A case study on high concentration solutions of a multi-domain protein

Pharmaceutical Research

Volumn 31, Issue 6, 2014, Pages 1575-1587

  Saluja, Atul ^a   Sadineni, Vikram ^a   Mungikar, Amol ^a   Nashine, Vishal ^a   Kroetsch, Andrew ^a   Dahlheim, Charles ^a   Rao, Venkatramana M ^a  

^a BRISTOL MYERS SQUIBB   (United States)

Author keywords

arrhenius kinetics; extended lumry eyring model; physical stability; protein aggregation; protein formulation; protein unfolding; shelf life; thermodynamics

Indexed keywords

MONOMER; HYBRID PROTEIN; SOLUTION AND SOLUBILITY;

ACCURACY; ARTICLE; CONCENTRATION (PARAMETERS); KINETICS; MATHEMATICAL MODEL; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN DOMAIN; PROTEIN REFOLDING; PROTEIN STABILITY; PROTEIN UNFOLDING; TEMPERATURE SENSITIVITY; THERMODYNAMICS; ALGORITHM; CHEMISTRY; DRUG EFFECTS; DRUG STORAGE; HUMAN; PROTEIN CONFORMATION; SOLUTION AND SOLUBILITY;

ALGORITHMS; DRUG STORAGE; HUMANS; KINETICS; PROTEIN CONFORMATION; PROTEIN UNFOLDING; RECOMBINANT FUSION PROTEINS; SOLUTIONS; THERMODYNAMICS;

EID: 84902214593     PISSN: 07248741     EISSN: 1573904X     Source Type: Journal    
DOI: 10.1007/s11095-013-1263-5     Document Type: Article

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