Correlations between changes in conformational dynamics and physical stability in a mutant IgG1 mAb engineered for extended serum half-life

mAbs

Volumn 7, Issue 1, 2015, Pages 84-95

  Majumdar, Ranajoy ^a   Esfandiary, Reza ^b   Bishop, Steven M ^b   Samra, Hardeep S ^b   Middaugh, C Russell ^a   Volkin, David B ^a   Weis, David D ^a  

^a UNIVERSITY OF KANSAS   (United States)

^b MEDIMMUNE   (United States)

Author keywords

Aggregation; Differential scanning calorimetry; Flexibility; Hydrogen deuterium exchange; Immunoglobulin G1; Mass spectrometry; Monoclonal antibody; Stability; YTE mutation

Indexed keywords

IMMUNOGLOBULIN G1 ANTIBODY; IMMUNOGLOBULIN G1 MONOCLONAL ANTIBODY; MONOCLONAL ANTIBODY; UNCLASSIFIED DRUG; IMMUNOGLOBULIN G;

AMINO ACID SEQUENCE; ARTICLE; DEGLYCOSYLATION; DEUTERIUM HYDROGEN EXCHANGE; DIFFERENTIAL SCANNING CALORIMETRY; DRUG CONFORMATION; DRUG HALF LIFE; DRUG STABILITY; GEL PERMEATION CHROMATOGRAPHY; INDUCED MUTATION; MASS SPECTROMETRY; MOLECULAR WEIGHT; OXIDATION; PH; POINT MUTATION; PROTEIN STABILITY; STORAGE; THERMOGRAPHY; THERMOSTABILITY; AMINO ACID SUBSTITUTION; CHEMISTRY; GENETICS; HALF LIFE TIME; KINETICS; MISSENSE MUTATION; OXIDATION REDUCTION REACTION; PROTEIN TERTIARY STRUCTURE; SERUM;

AMINO ACID SUBSTITUTION; ANTIBODIES, MONOCLONAL; HALF-LIFE; IMMUNOGLOBULIN G; KINETICS; MUTATION, MISSENSE; OXIDATION-REDUCTION; PROTEIN STABILITY; PROTEIN STRUCTURE, TERTIARY; SERUM;

EID: 84921340583     PISSN: 19420862     EISSN: 19420870     Source Type: Journal    
DOI: 10.4161/19420862.2014.985494     Document Type: Article

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