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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.