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Effect of pegylation on pharmaceuticals
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Journal Article
Effect of pegylation on pharmaceuticals
2003
Overview
Key Points
Polypeptides that are being discovered by the biotechnology industry hold great promise as new drug candidates to target specific disease symptoms.
However, polypeptide drugs are rapidly degraded by proteolytic enzymes and neutralized by antibodies, among other shortcomings. This reduces their half-life and circulation time, thereby limiting their therapeutic effectiveness.
Pegylation of polypeptide drugs protects them and improves their pharmacodynamic and pharmacokinetic profiles.
The pegylation process attaches repeating units of polyethylene glycol (PEG) to a polypeptide drug. For the past 30 years, scientists have improved various chemistries to build PEG polymers and attach them to a polypeptide drug of choice.
Among the first pegylated drugs approved by the FDA in the early 1990s were pegaspargase for leukemia and pegademase for severe combined immunodeficiency disorder. More recently, pegylated drugs for the treatment of hepatitis C, acromegaly, rheumatoid arthritis, neutropenia, various cancers, wound healing, and other disorders either have been approved or are undergoing clinical trials.
Researchers will continue to perfect the chemistries employed in pegylation to develop more polypeptide therapeutic products.
Protein and peptide drugs hold great promise as therapeutic agents. However, many are degraded by proteolytic enzymes, can be rapidly cleared by the kidneys, generate neutralizing antibodies and have a short circulating half-life. Pegylation, the process by which polyethylene glycol chains are attached to protein and peptide drugs, can overcome these and other shortcomings. By increasing the molecular mass of proteins and peptides and shielding them from proteolytic enzymes, pegylation improves pharmacokinetics. This article will review how PEGylation can result in drugs that are often more effective and safer, and which show improved patient convenience and compliance.
Publisher
Nature Publishing Group UK,Nature Publishing Group
