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Acylated heptapeptide binds albumin with high affinity and application as tag furnishes long-acting peptides.

Nature communications (2017-07-18)
Alessandro Zorzi, Simon J Middendorp, Jonas Wilbs, Kaycie Deyle, Christian Heinis
RESUMEN

The rapid renal clearance of peptides in vivo limits this attractive platform for the treatment of a broad range of diseases that require prolonged drug half-lives. An intriguing approach for extending peptide circulation times works through a 'piggy-back' strategy in which peptides bind via a ligand to the long-lived serum protein albumin. In accordance with this strategy, we developed an easily synthesized albumin-binding ligand based on a peptide-fatty acid chimera that has a high affinity for human albumin (K

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Sigma-Aldrich
Suero humano, from human male AB plasma, USA origin, sterile-filtered
Sigma-Aldrich
Albúmina from human serum, lyophilized powder, ≥96% (agarose gel electrophoresis)
Sigma-Aldrich
Albumin from rat serum, lyophilized powder, ≥96% (agarose gel electrophoresis)
Sigma-Aldrich
Albumin from rabbit serum, lyophilized powder, ≥96% (agarose gel electrophoresis)