For Research Use Only. Not for Clinical Use.

Albumin is ideally suited as a half-life extension module with a half-life of approximately 19 days in vivo. The drug's pharmacokinetic properties can be improved by reversibly binding on albumin expediently. In recent years, Creative Biolabs has developed different strategies of half-life extension service by non-covalent binding of therapeutic molecules to albumin widely used in both proteins and small chemical medicine. It's our pleasure to support your research with these services.

Introduction of Non-Covalent Binding of Therapeutic Molecules to Albumin

It is well known that albumin acts as a transporter, reversibly binding to a broad range of endogenous or exogenous ligands, peptides, and proteins. This binding affects the pharmacokinetic properties of these molecules, typically enhancing their distribution and bioavailability. Therefore, indirect binding can be achieved by conjugating albumin to peptide therapeutic with the help of a helper molecule, for example, attaching fatty-chain by non-covalent binding. Non-covalent association with serum albumin allows for a dissociation of the therapeutic protein from albumin, which can be advantageous by facilitating extravasation and tissue penetration. This method has been employed in many protein drugs approved or in clinical trials owing to its high security and low immunogenicity.

Fig.1 FcRn mediated albumin recycling with drug attached (green molecule). (Sleep, 2013)

Application of Half-Life Extension Services by Non-Covalent Binding of Therapeutic Molecules to Albumin

Due to Extensive combination ability, there are a lot of non-covalent binding strategies of drugs to albumin depending on various modification processes such as lipidation or helper molecules, by using albumin-binding domains (ABD), or albumin binding domain antibody (AlbudAb). Depending on the research of protein engineering, a series of proteins drugs are produced under good manufacturing practice (GMP) conditions and launch on the market.

Many famous peptide therapeutic formulations developed exploiting non-covalent binding of therapeutic molecules to albumin technology eventually went to clinical application. Two typical examples of approved drugs modification are bounded myristic acid to insulin or glucagon-like peptide-1(GLP-1) agonist and extended its half-life by a hundred times, relying on the ability of albumin to bind fatty acids. With the tremendous commercial success of these two drugs, there are increasing studies on non-covalent binding strategies of therapeutic molecules to albumin that generally extend the half-life by more than 50 times.

What Can We Do?

The key of achieve half-life extension in the mentioned method is the selection of suitable helper molecules to match the target drugs. Creative Biolabs offers half-life extension services by non-covalent binding of therapeutic molecules to albumin by various means to support your drug research.

Reference

1. Sleep, D.; et al. Albumin as a versatile platform for drug half-life extension. Biochimica Et Biophysica Acta. 2013, 1830(12): 5526-5534.

Related Services:

• Half-Life Extension by Lipidation
• Albumin-Binding Domain Based Half-Life Extension
• AlbudAb Based Half-Life Extension Services