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The team achieved this by replacing cysteine’s single sulfur group with a branch comprising two sulfur organizations. After synthesizing the five brand-new amino acids, the team integrated them in to the framework of two bioactive peptides, one that inhibits an enzyme implicated in cancers, and one blocking a receptor within neurons. Testing just a handful of cyclic peptides with the synthetic amino acid, Heinis’ team could identify several peptides that showed enhanced activities. The best inhibitor of the neuron receptor was 8-fold improved and the best protease inhibitor got a good 40-fold higher activity.