期刊
NATURE CHEMISTRY
卷 4, 期 1, 页码 60-64出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/nchem.1213
关键词
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资金
- Office of Naval Research [N000140910137, N000141010600]
- National Science Foundation [DMR-1005699]
- National Cancer Institute [T32CA138312]
- NATIONAL CANCER INSTITUTE [T32CA138312] Funding Source: NIH RePORTER
Treatment with therapeutic proteins is an attractive approach to targeting a number of challenging diseases. Unfortunately, the native proteins themselves are often unstable in physiological conditions, reducing bioavailability and therefore increasing the dose that is required. Conjugation with poly(ethylene glycol) (PEG) is often used to increase stability, but this has a detrimental effect on bioactivity. Here, we introduce conjugation with zwitterionic polymers such as poly(carboxybetaine). We show that poly(carboxybetaine) conjugation improves stability in a manner similar to PEGylation, but that the new conjugates retain or even improve the binding affinity as a result of enhanced protein-substrate hydrophobic interactions. This chemistry opens a new avenue for the development of protein therapeutics by avoiding the need to compromise between stability and affinity.
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