| Literature DB >> 12574628 |
Gerd G Kochendoerfer1, Shiah-Yun Chen, Feng Mao, Sonya Cressman, Stacey Traviglia, Haiyan Shao, Christie L Hunter, Donald W Low, E Neil Cagle, Maia Carnevali, Vincent Gueriguian, Peter J Keogh, Heather Porter, Stephen M Stratton, M Con Wiedeke, Jill Wilken, Jie Tang, Jay J Levy, Les P Miranda, Milan M Crnogorac, Suresh Kalbag, Paolo Botti, Janice Schindler-Horvat, Laura Savatski, John W Adamson, Ada Kung, Stephen B H Kent, James A Bradburne.
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.Entities:
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Year: 2003 PMID： 12574628 DOI： 10.1126/science.1079085
Source DB: PubMed Journal: Science ISSN： 0036-8075 Impact factor: 47.728