期刊
ACTA NATURAE
卷 8, 期 4, 页码 70-81出版社
RUSSIAN FEDERATION AGENCY SCIENCE & INNOVATION
DOI: 10.32607/20758251-2016-8-4-70-81
关键词
alpha-helix; conformational stability; factors of thermal stability; membrane permeability; resistance to intracellular proteolysis
资金
- Russian Science Foundation [14-34-00023]
- Russian Science Foundation [14-34-00023] Funding Source: Russian Science Foundation
alpha-Heli.es are the most frequently occurring elements of the secondary structure in water-soluble globular proteins. Their increased conformational stability is among the main reasons for the high thermal stability of proteins in thermophilic bacteria. In addition, alpha-helices are often involved in protein interactions with other proteins, nucleic acids, and the lipids of cell membranes. That is why the highly stable alpha-helical peptides used as highly active and specific inhibitors of protein-protein and other interactions have recently found more applications in medicine. Several different approaches have been developed in recent years to improve the conformational stability of alpha-helical peptides and thermostable proteins, which will be discussed in this review. We also discuss the methods for improving the permeability of peptides and proteins across cellular membranes and their resistance to intracellular protease activity. Special attention is given to the SEQOPT method (http://mml.spbstu.ru/services/seqopt/), which is used to design conformationally stable short alpha-helices.
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