Comparative Analysis of Glycoform Profiles Between Biosimilar and Originator Monoclonal Antibodies by Liquid Chromatography–Mass Spectrometry

Ahmet Emin Atik

Makale detayları

Comparative Analysis of Glycoform Profiles Between Biosimilar and Originator Monoclonal Antibodies by Liquid Chromatography–Mass Spectrometry

Yazarlar:

Ahmet Emin Atik

Yayıncı:

Turkish Chemical Society

Ana Başlıklar:

Analytical Chemistry

Dergi:

Journal of the Turkish Chemical Society Section A: Chemistry Vol.11 Issue 1, pp.365-376

Belge Tipi:

Makale

Yayın Tarihi:

4/2024

Belge Dili:

İngilizce

Document ID (Org No.):

2001303729

pISSN:

2149-0120

Anahtar kelimeler:

Özet:

 Glycosylation is considered as a critical quality attribute for monoclonal antibodies mAbs and needs routine monitoring during production. This study aims to compare the glycoform profiles of biosimilar and four originator mAbs using ultra-performance liquid chromatography UPLC coupled to electrospray ionization-quadrupole time of flight-mass spectrometry ESIQ-TOF MS. The resultant mass spectrum showed that seven different glycoform pairs, including G0FGNG0, G0FGNG0F, G0FG0F, G0FG1F, G1FG1F, G1FG2F, and G2FG2F were identified via intact mass analysis for all tested mAb samples. The correct identification of each glycoform pair was achieved by comparing the observed mass with its theoretical mass using high-resolution mass spectrometry data with mass accuracies of less than 100 ppm. The most abundant paired glycoforms detected at the intact protein level are G0FG0F and G0FG1F, with relative abundance ranges of 38.45  43.43 and 19.32  22.20, respectively. The obtained data demonstrated that biosimilar and originators have the same types of glycoform pairs, and the relative abundances of each pair were comparable among biosimilar and four originator mAb samples. Additionally, the reduced mass analysis revealed that five different glycans G0FGN, G0, G0F, G1F, and G2F were attached to the heavy chain of the mAb, and the relative abundance of G0F ranged from 75.21 to 77.90. The detected mass accuracies for reduced mass analysis were below 25 ppm. The results of the intact and reduced mass analyses showed that the biosimilar is similar to its originator in terms of glycoform percentages and molecular masses.

 Glycosylation is considered as a critical quality attribute for monoclonal antibodies mAbs and needs routine monitoring during production. This study aims to compare the glycoform profiles of biosimilar and four originator mAbs using ultra-performance liquid chromatography UPLC coupled to electrospray ionization-quadrupole time of flight-mass spectrometry ESIQ-TOF MS. The resultant mass spectrum showed that seven different glycoform pairs, including G0FGNG0, G0FGNG0F, G0FG0F, G0FG1F, G1FG1F, G1FG2F, and G2FG2F were identified via intact mass analysis for all tested mAb samples. The correct identification of each glycoform pair was achieved by comparing the observed mass with its theoretical mass using high-resolution mass spectrometry data with mass accuracies of less than 100 ppm. The most abundant paired glycoforms detected at the intact protein level are G0FG0F and G0FG1F, with relative abundance ranges of 38.45  43.43 and 19.32  22.20, respectively. The obtained data demonstrated that biosimilar and originators have the same types of glycoform pairs, and the relative abundances of each pair were comparable among biosimilar and four originator mAb samples. Additionally, the reduced mass analysis revealed that five different glycans G0FGN, G0, G0F, G1F, and G2F were attached to the heavy chain of the mAb, and the relative abundance of G0F ranged from 75.21 to 77.90. The detected mass accuracies for reduced mass analysis were below 25 ppm. The results of the intact and reduced mass analyses showed that the biosimilar is similar to its originator in terms of glycoform percentages and molecular masses.

 Glycosylation is considered as a critical quality attribute for monoclonal antibodies mAbs and needs routine monitoring during production. This study aims to compare the glycoform profiles of biosimilar and four originator mAbs using ultra-performance liquid chromatography UPLC coupled to electrospray ionization-quadrupole time of flight-mass spectrometry ESIQ-TOF MS. The resultant mass spectrum showed that seven different glycoform pairs, including G0FGNG0, G0FGNG0F, G0FG0F, G0FG1F, G1FG1F, G1FG2F, and G2FG2F were identified via intact mass analysis for all tested mAb samples. The correct identification of each glycoform pair was achieved by comparing the observed mass with its theoretical mass using high-resolution mass spectrometry data with mass accuracies of less than 100 ppm. The most abundant paired glycoforms detected at the intact protein level are G0FG0F and G0FG1F, with relative abundance ranges of 38.45  43.43 and 19.32  22.20, respectively. The obtained data demonstrated that biosimilar and originators have the same types of glycoform pairs, and the relative abundances of each pair were comparable among biosimilar and four originator mAb samples. Additionally, the reduced mass analysis revealed that five different glycans G0FGN, G0, G0F, G1F, and G2F were attached to the heavy chain of the mAb, and the relative abundance of G0F ranged from 75.21 to 77.90. The detected mass accuracies for reduced mass analysis were below 25 ppm. The results of the intact and reduced mass analyses showed that the biosimilar is similar to its originator in terms of glycoform percentages and molecular masses.

 Glycosylation is considered as a critical quality attribute for monoclonal antibodies mAbs and needs routine monitoring during production. This study aims to compare the glycoform profiles of biosimilar and four originator mAbs using ultra-performance liquid chromatography UPLC coupled to electrospray ionization-quadrupole time of flight-mass spectrometry ESIQ-TOF MS. The resultant mass spectrum showed that seven different glycoform pairs, including G0FGNG0, G0FGNG0F, G0FG0F, G0FG1F, G1FG1F, G1FG2F, and G2FG2F were identified via intact mass analysis for all tested mAb samples. The correct identification of each glycoform pair was achieved by comparing the observed mass with its theoretical mass using high-resolution mass spectrometry data with mass accuracies of less than 100 ppm. The most abundant paired glycoforms detected at the intact protein level are G0FG0F and G0FG1F, with relative abundance ranges of 38.45  43.43 and 19.32  22.20, respectively. The obtained data demonstrated that biosimilar and originators have the same types of glycoform pairs, and the relative abundances of each pair were comparable among biosimilar and four originator mAb samples. Additionally, the reduced mass analysis revealed that five different glycans G0FGN, G0, G0F, G1F, and G2F were attached to the heavy chain of the mAb, and the relative abundance of G0F ranged from 75.21 to 77.90. The detected mass accuracies for reduced mass analysis were below 25 ppm. The results of the intact and reduced mass analyses showed that the biosimilar is similar to its originator in terms of glycoform percentages and molecular masses.

Makale detayları

Comparative Analysis of Glycoform Profiles Between Biosimilar and Originator Monoclonal Antibodies by Liquid Chromatography–Mass Spectrometry

Yazarlar:

Ahmet Emin Atik

Yayıncı:

Turkish Chemical Society

Ana Başlıklar:

Analytical Chemistry

Dergi:

Journal of the Turkish Chemical Society Section A: Chemistry Vol.11 Issue 1, pp.365-376

Belge Tipi:

Makale

Yayın Tarihi:

4/2024

Belge Dili:

İngilizce

Document ID (Org No.):

2001303729

pISSN:

2149-0120

Biosimilar

monoclonal antibody

glycoform

liquid chromatography-mass spectrometry

Sayı

Makale detayları

Comparative Analysis of Glycoform Profiles Between Biosimilar and Originator Monoclonal Antibodies by Liquid Chromatography–Mass Spectrometry

Yazarlar: Ahmet Emin Atik

Yayıncı: Turkish Chemical Society

Ana Başlıklar: Analytical Chemistry

Dergi: Journal of the Turkish Chemical Society Section A: Chemistry Vol.11 Issue 1, pp.365-376

Belge Tipi: Makale

Yayın Tarihi: 4/2024

Belge Dili: İngilizce

Document ID (Org No.): 2001303729

pISSN: 2149-0120

Biosimilar

monoclonal antibody

glycoform

liquid chromatography-mass spectrometry

Sayı

Yazarlar:

Ahmet Emin Atik

Yayıncı:

Turkish Chemical Society

Ana Başlıklar:

Analytical Chemistry

Dergi:

Journal of the Turkish Chemical Society Section A: Chemistry Vol.11 Issue 1, pp.365-376

Belge Tipi:

Makale

Yayın Tarihi:

4/2024

Belge Dili:

İngilizce

Document ID (Org No.):

2001303729

pISSN:

2149-0120