Structural highlights
Function
TRY1_BOVIN
Publication Abstract from PubMed
Engineering biosynthetic pathways to ribosomally synthesized and post-translationally modified peptides (RiPPs) offers several advantages for both in vivo and in vitro applications. Here we probe the ability of peptide cyclases to generate trimacrocycle microviridin analogs with non-native cross-links. The results demonstrate that diverse chemistries are tolerated by macrocyclases in the ATP-grasp family and allow for the construction of unique cyclic peptide architectures that retain protease inhibition activity. In addition, cocomplex structures of analogs bound to a model protease were determined, illustrating how changes in functional groups maintain peptide conformation and target binding.
Alternative Linkage Chemistries in the Chemoenzymatic Synthesis of Microviridin-Based Cyclic Peptides.,Patel KP, Chen WT, Delbecq L, Bruner SD Org Lett. 2024 Feb 16;26(6):1138-1142. doi: 10.1021/acs.orglett.3c04045. Epub , 2024 Feb 2. PMID:38306609[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Patel KP, Chen WT, Delbecq L, Bruner SD. Alternative Linkage Chemistries in the Chemoenzymatic Synthesis of Microviridin-Based Cyclic Peptides. Org Lett. 2024 Feb 16;26(6):1138-1142. PMID:38306609 doi:10.1021/acs.orglett.3c04045
