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Cited by 2Protein Structure and DynamicsEnzyme Structure and FunctionGlycosylation and Glycoproteins Research

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SAXS data based glycosylated models of human alpha-1-acid glycorprotein, a key player in health, disease and drug circulation

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Kalidas, Nidhi, Peddada, Nagesh, Pandey, Kalpana, Ashish·2026·Journal of Biomolecular Structure and Dynamics
DOI 10.1080/07391102.2025.2475244

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Abstract

Plasma Alpha-1-glycoprotein (AGP) binds diverse drugs, its isoforms and their levels vary significantly in acute phases of health. Relative binding pattern of drugs to AGP and albumin has been used to model their release profiles, and structural insights on glycosylated form of AGP will improve predictions. Main challenge is the heavy and heterogeneous glycosylation of AGP molecules. Our small angle X-ray scattering (SAXS) data on plasma extracted AGP showed interparticulate effect from 283 to 313 K which disappeared irreversibly upon further heating to 343K. Using ALPHAFOLD2 server, the protein only portion could be modelled but as expected its theoretical SAXS profile did not match acquired experimental data. Using mass spectra-based information, we attached representative glycan motifs at known sites to compute four models of fully glycosylated AGP. Importantly, calculated SAXS profiles of these models agreed with our experimental data. These representative glycosylated models were further analyzed for molecular motions using Normal Mode Analysis and all-atom Molecular Dynamics simulations in reference to SAXS data. Overall, we show that SAXS data-based models of glycoprotein are better representation of this biopharmaceutical molecule and provide them for structure-based drug profile estimations.

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Metadata

Authors
Kalidas, N., Peddada, N., Pandey, K., & Ashish
Affiliations
Institute of Microbial Technology (IN)
Corresponding author
Ashish
ORCID
Venue
Journal of Biomolecular Structure and Dynamics
Publisher
Informa UK Limited
Published
2025-03-08
Volume
44
Issue
5
Pages
2709-2723
ISSN
  • 0739-1102 (ISSN-L)
  • 1538-0254
DOI
10.1080/07391102.2025.2475244
OpenAlex
W4408249118
Cited by
2
References
1
Citations by year
2026: 1 · 2025: 1
FWCI
0.60
Type
journal article
Language
en
Open access
Locations
  • Journal of Biomolecular Structure and Dynamics (publishedVersion)
  • bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion)
  • PubMed (publishedVersion)
Funders
CSIR – Institute of Microbial Technology
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glycosylation and Glycoproteins Research
Keywords
alpha-1-acid glycoprotein, plasma glycoproteins, glycosylation, drug binding, albumin, drug release profile, protein conformational dynamics
MeSH terms
Glycosylation, Humans, Models, Molecular, Orosomucoid, Protein Conformation, X-Ray Diffraction, Scattering, Small Angle, Molecular Dynamics Simulation

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