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Communications

Impact of base matrix types on the properties of affinity chromatography resins with ligands based on staphylococcal protein A B-domain multimers

M. V. Baskovaab, M. N. Tereshina, Kh. P. Telepeninaa, N. S. Shoshinaa, A. M. Komyakovaab, B. Z. Eletskayac, M. Ya. Berzinaac, L. N. Ikryannikovaa, V. N. Stepanenkoab, T. D. Melikhovaac

a I. M. Sechenov First Moscow State Medical University, 119991 Moscow, Russian Federation
b M. V. Lomonosov Institute of Fine Chemical Technologies, MIREA – Russian Technological University, 119571 Moscow, Russian Federation
c M. M. Shemyakin–Yu. A. Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, 117437 Moscow, Russian Federation


Аннотация: New chromatography resins with ligands based on oligomers of the B-domain of Staphylococcus aureus protein A were developed and characterized. Resin performance, particularly dynamic binding capacity, improved as the ligand length increased from dimer to tetramer when immobilized on a polymethacrylate surface, whereas the opposite effect was observed when using cross-linked agarose as a matrix. It was found that particle size uniformity and pore volume can play a significant role and their careful control is necessary when selecting a matrix.

Ключевые слова: Staphylococcus aureus protein A, SpA, IgG binding domains B, B-domains, affinity chromatography, domain oligomerization, polymethacrylate beads, agarose matrix.

Поступила в редакцию: 21.11.2025
Принята в печать: 12.02.2026

Язык публикации: английский

DOI: 10.71267/mencom.7973



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