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

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

Majumdar, Ranajoy; Esfandiary, Reza; Bishop, Steven M; Samra, Hardeep S; Middaugh, C Russell; Volkin, David B; Weis, David D.

Affiliation

Majumdar R; a Department of Pharmaceutical Chemistry ; University of Kansas ; Lawrence , KS USA.

MAbs ; 7(1): 84-95, 2015.

Article in En | MEDLINE | ID: mdl-25524268

Subject(s)
Key words

CH1-CH3, constant domains 13, respectively, of the heavy chain of a monoclonal antibody; DSC, differential scanning calorimetry; Fab, antigen binding fragment of a monoclonal antibody; Fc, crystallizable fragment of a monoclonal antibody; HC, heavy chain of a monoclonal antibody; HX-MS, hydrogen/deuterium exchange mass spectrometry; LC, light chain of a monoclonal antibody; VH/VL, variable domain of the heavy/light chain of a monoclonal antibody; YTE mutation; aggregation; differential scanning calorimetry; flexibility; hydrogen/deuterium exchange; immunoglobulin G1; mass spectrometry; monoclonal antibody; stability

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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Immunoglobulin G / Amino Acid Substitution / Mutation, Missense / Antibodies, Monoclonal Language: En Journal: MAbs Journal subject: ALERGIA E IMUNOLOGIA Year: 2015 Document type: Article Country of publication:

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