期刊
BIOPOLYMERS
卷 98, 期 3, 页码 195-211出版社
WILEY
DOI: 10.1002/bip.22030
关键词
N-glycosylation; enhanced aromatic sequons; glycoproteins
资金
- Skaggs Institute for Chemical Biology
- Lita Annenberg Hazen Foundation
- National Institutes of Health (NIH) [GM051105, AI072155, F32 GM086039]
N-glycosylation can increase the rate of protein folding, enhance thermodynamic stability, and slow protein unfolding; however, the molecular basis for these effects is incompletely understood. Without clear engineering guidelines, attempts to use N-glycosylation as an approach for stabilizing proteins have resulted in unpredictable energetic consequences. Here, we review the recent development of three enhanced aromatic sequons, which appear to facilitate stabilizing native-state interactions between Phe, Asn-GlcNAc and Thr when placed in an appropriate reverse turn context. It has proven to be straightforward to engineer a stabilizing enhanced aromatic sequon into glycosylation-naive proteins that have not evolved to optimize specific proteincarbohydrate interactions. Incorporating these enhanced aromatic sequons into appropriate reverse turn types within proteins should enhance the well-known pharmacokinetic benefits of N-glycosylation-based stabilization by lowering the population of protease-susceptible unfolded and aggregation-prone misfolded states, thereby making such proteins more useful in research and pharmaceutical applications. (c) 2011 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 98: 195211, 2012.
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