期刊
FUTURE MEDICINAL CHEMISTRY
卷 5, 期 18, 页码 2175-2183出版社
FUTURE SCI LTD
DOI: 10.4155/fmc.13.179
关键词
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The most abundant protein secondary structure in nature - the -helix - is frequently found at protein interfaces, making it an important lead structure for the design of small-molecule modulators of protein-protein interactions (PPIs). Nature's ability to precisely control the length of -helices, especially in the context of helix-mediated PPIs, is key to ensuring the optimal interaction of protein partners. By extension, precise control over the length of -helix mimetics is necessary to ensure optimal disruption of -helix-mediated PPIs. This article will highlight the emerging importance of helix length control in the context of helix-mediated PPIs through a discussion of the contemporary chemical approaches to identifying novel helix mimetic inhibitors, including all-hydrocarbon stapling, hydrogen bond surrogates and optimized peptides emerging from in vitro screening methods. A current update on the therapeutic status of the different approaches is provided, as well as indications as to their long-term potential.
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