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PEGylation Products and Services

PEGylation Products and Services

Introducing polyethylene glycol (PEG) to biomolecules and pharmaceuticals is known to enhance stability and pharmacological properties of proteins, peptides, antibody-drug conjugates and small-molecule drugs. As a synthetic polymer with high hydrophilicity, PEG is widely used to prolong circulation time of proteins, increase aqueous solubility of therapeutic molecules and reduce immunogenicity of biopharmaceuticals. To date, PEGylation has been successfully used in 12 marketed drugs.1 The PEGylation technology, first used in protein modification, has been recently transferred to small-molecule drugs, leading to a new wave of investigation in pharmaceutical industry.

The two major types of PEG reagents, linear PEG and branched PEG, are both used in marketed drugs. Linear PEG reagents provide for single, low PEG density modification per attachment, whereas conjugation with branched or multi-arm PEG reagents results in high PEG density per modification, which might be advantageous if mono-PEGylation is applied. The attachment of PEG to proteins usually involves reactions with amino acid side chains such as lysine, cysteine and N-terminal amine for their relatively high reactivity. To avoid affecting protein functions, mono-PEGylation and site-specific PEGylation are preferred as they deliver PEG reagents to defined locations to minimize the change of protein structure and to simplify purification process.

With years of experience in bioconjugation services, Profacgen provides a full spectrum of quality solutions, from single reagents to comprehensive PEGylation service, to meet your specific needs.

Please contact us for more information regarding our PEGylation products and services. Our representatives are available 24 hours a day, Monday through Friday, to assist you.

References:

1. Turecek, P.; et al. PEGylation of Biopharmaceuticals: A Review of Chemistry and Nonclinical Safety Information of Approved Drugs. Journal of Pharmaceutical Sciences 2016, 105(42): 460 - 475

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