College of Chemistry, Chemical Engineering and Materials Science, Collaborative Innovation Center of Functionalized Probes for Chemical Imaging in Universities of Shandong, Key Laboratory of Molecular and Nano Probes, Ministry of Education, Shandong Provincial Key Laboratory of Clean Production of Fine Chemicals , Shandong Normal University , Jinan 250014 , People's Republic of China.
Anal Chem. 2018 Aug 7;90(15):9523-9528. doi: 10.1021/acs.analchem.8b02228. Epub 2018 Jul 9.
The sulfilimine bond (-S═N-), found in the collagen IV scaffold, significantly stabilizes the architecture via the formation of sulfilimine cross-links. However, precisely governing the formation and breakup process of the sulfilimine bond in living organisms for better life functions still remains a challenge. Hence, we established a new way to regulate the breaking and formation of the sulfilimine bond through hydrogen selenide (HSe) and hypobromous acid (HOBr), which can be easily controlled at simulated physiological conditions. This novel strategy provides a circulation regulation system to modulate the sulfilimine bond in peptides and NC1 hexamers, which can offer a substantial system for further study of the physiological function of collagen IV.
存在于 IV 型胶原支架中的亚磺酰亚胺键 (-S═N-) 通过形成亚磺酰亚胺交联显著稳定了结构。然而，为了更好地实现生命功能，精确控制亚磺酰亚胺键在生物体内的形成和断裂过程仍然是一个挑战。因此，我们建立了一种新的方法，通过硒化氢 (HSe) 和次溴酸 (HOBr) 来调节亚磺酰亚胺键的断裂和形成，这可以在模拟生理条件下轻松控制。这种新策略提供了一种循环调节系统来调节肽和 NC1 六聚体中的亚磺酰亚胺键，这为进一步研究 IV 型胶原的生理功能提供了一个重要的系统。
