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  • Title: Design and chemical synthesis of a homogeneous polymer-modified erythropoiesis protein.
    Author: Kochendoerfer GG, Chen SY, Mao F, Cressman S, Traviglia S, Shao H, Hunter CL, Low DW, Cagle EN, Carnevali M, Gueriguian V, Keogh PJ, Porter H, Stratton SM, Wiedeke MC, Wilken J, Tang J, Levy JJ, Miranda LP, Crnogorac MM, Kalbag S, Botti P, Schindler-Horvat J, Savatski L, Adamson JW, Kung A, Kent SB, Bradburne JA.
    Journal: Science; 2003 Feb 07; 299(5608):884-7. PubMed ID: 12574628.
    Abstract:
    We report the design and total chemical synthesis of "synthetic erythropoiesis protein" (SEP), a 51-kilodalton protein-polymer construct consisting of a 166-amino-acid polypeptide chain and two covalently attached, branched, and monodisperse polymer moieties that are negatively charged. The ability to control the chemistry allowed us to synthesize a macromolecule of precisely defined covalent structure. SEP was homogeneous as shown by high-resolution analytical techniques, with a mass of 50,825 +/-10 daltons by electrospray mass spectrometry, and with a pI of 5.0. In cell and animal assays for erythropoiesis, SEP displayed potent biological activity and had significantly prolonged duration of action in vivo. These chemical methods are a powerful tool in the rational design of protein constructs with potential therapeutic applications.
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