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Differential glycosylation does not modulate the conformational heterogeneity of a humanised IgGk NIST monoclonal antibody.
Liu, Fanny C; Lee, Jusung; Pedrete, Thais; Panczyk, Erin M; Pengelley, Stuart; Bleiholder, Christian.
Afiliación
  • Liu FC; Department of Chemistry and Biochemistry, Florida State University, 102 Varsity Way, Tallahassee, Florida, 32306, USA. cbleiholder@fsu.edu.
  • Lee J; Department of Chemistry and Biochemistry, Florida State University, 102 Varsity Way, Tallahassee, Florida, 32306, USA. cbleiholder@fsu.edu.
  • Pedrete T; Department of Chemistry and Biochemistry, Florida State University, 102 Varsity Way, Tallahassee, Florida, 32306, USA. cbleiholder@fsu.edu.
  • Panczyk EM; Bruker Daltonics, 40 Manning Road, Billerica, MA 01821, USA.
  • Pengelley S; Bruker Daltonics GmbH&Co, Fahrenheitstrasse 4, Bremen, 28359, Germany.
  • Bleiholder C; Department of Chemistry and Biochemistry, Florida State University, 102 Varsity Way, Tallahassee, Florida, 32306, USA. cbleiholder@fsu.edu.
Chem Commun (Camb) ; 60(77): 10740-10743, 2024 Sep 24.
Article en En | MEDLINE | ID: mdl-39246094
ABSTRACT
Investigating the structural heterogeneity of monoclonal antibodies is crucial to achieving optimal therapeutic outcomes. We show that tandem-trapped ion mobility spectrometry enables collision-induced unfolding measurements of subpopulations of a humanised IgGk NIST monoclonal antibody (NISTmAb). Our results indicate that differential glycosylation of NISTmAb does not modulate its conformational heterogeneity.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Inmunoglobulina G / Anticuerpos Monoclonales Límite: Humans Idioma: En Revista: Chem Commun (Camb) Asunto de la revista: QUIMICA Año: 2024 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Reino Unido
Texto completo
Añadir a Mi BVS
Imprimir
XML
PubMed Links
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Inmunoglobulina G / Anticuerpos Monoclonales Límite: Humans Idioma: En Revista: Chem Commun (Camb) Asunto de la revista: QUIMICA Año: 2024 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Reino Unido