Protecting Groups

Boc-D-Tyr(tBu)-OH is a natural product that is an amphipathic molecule with a cyclic structure. It has been shown to be able to inhibit the growth of bacteria, such as Staphylococcus aureus and Escherichia coli, by acting as an antibiotic. Boc-D-Tyr(tBu)-OH inhibits the synthesis of peptides by binding to the ribosome and blocking peptide elongation. This molecule also inhibits peptide synthesis by interacting with the aminoacyl site on the ribosome and preventing it from binding with amino acids. Boc-D-Tyr(tBu)-OH is synthesized in two stages: solid phase peptide synthesis and nucleophilic activation. The decapeptides are then purified and characterized based on their function.

4-tert-Butyl-L-phenylalanine is a synthetically created antigen with the ability to interact with red blood cells. It has been shown to be a potent probe for the detection of P. falciparum, and can be used as an affinity reagent for the isolation and identification of mutations in the c-terminal region of this protein. 4-tert-Butyl-L-phenylalanine also interacts with P. falciparum apical membrane proteins, which are specific to this type of parasite. This interaction may play a role in its invasion into red blood cells, which is what causes malaria infection.

Fmoc-glycinol is a synthetase that is used to synthesize glycinol conjugates. It binds to the receptor on Gram-positive bacteria and blocks the synthesis of bacterial cell wall, leading to cell death. Fmoc-glycinol has been shown to have high binding constants with amines and an acyl chain, which allows it to bind with antigen. Fmoc-glycinol also has strong nucleophilic properties that allow it to react with chloride ions in water and other polar solvents. This reaction mechanism leads to the formation of a new bond between two molecules, which is called a glycinol linkage.