Noticing the hydrophobic properties of the silyl groups, we developed super silyl groups as hydrophobic tags to install at both the C- and N-terminals of peptides to enhance the solubility in liquid-phase peptide synthesis.
Development of a new hydrophobic auxiliary, TCbz group at the N-terminus of peptides is disclosed. This auxiliary enabled C-terminal modification in LPPS and a de novo solid/hydrophobic-tag relay synthesis (STRS) of calpinactam.
Here, we disclose the first total synthesis of tetraselide and determination of its absolute structure. We implemented bioinformatic analyses, chemical degradation, chiral pool fragment synthesis and convergent synthesis of this natural product.
Degrons are regions of a protein that are required to initiate their degradation by cellular machinery.
L12, derived from HyTTD, exhibits potent antiviral activity against oseltamivir-resistant influenza strains. L12 degrades the NA protein through ubiquitination to exert its anti-H1N1-H274Y activity.