Faculty of Chemistry, University of Wrocław, F. Joliot-Curie 14, 50383, Wrocław, Poland.
Faculty of Chemistry, Jagiellonian University, Gronostajowa 2, 30387, Kraków, Poland.
Chemistry. 2023 Jul 14;29(40):e202301370. doi: 10.1002/chem.202301370. Epub 2023 May 25.
Stabilization of a peptide conformation via stapling strategy may be realized by the reversible or more often irreversible connection of side chains being in mutually appropriate geometry. An incorporation of phenylboronic acid and sugar residues (fructonic or galacturonic acid), attached to two lysine side chains via amide bonds and separated by 2, 3, or 6 other residues in the C-terminal fragment of RNase A introduces the intramolecular interaction stabilizing the α-helical organization. The boronate ester stapling is stabilized in mild basic conditions and may be switched off by acidification leading to unfolded organization of the peptide chain. We investigated the possibility of using switchable stapling by mass spectrometry, NMR and UV-CD spectroscopies, and DFT calculations.
通过侧链的可逆或更常见的不可逆连接实现肽构象的稳定化，这些侧链处于相互适当的几何形状。通过酰胺键将苯硼酸和糖残基（果糖或半乳糖酸）连接到两个赖氨酸侧链上，并在核糖核酸酶 A 的 C 末端片段中相隔 2、3 或 6 个其他残基，引入了稳定 α-螺旋构象的分子内相互作用。硼酸盐酯键在温和的碱性条件下稳定，并可通过酸化关闭，导致肽链展开。我们通过质谱、NMR 和 UV-CD 光谱以及 DFT 计算研究了使用可切换键合的可能性。
