Acid fuels the motion of a threaded ring: A central goal in the construction of molecular-scale machines is the efficient achievement of one-way motion. Erbas-Cakmak et al. developed a class of machines that transmit pH changes into the two-stage guided motion of molecular rings threaded on a linear or cyclic axle. The design relies on temporary blocking groups and landing sites along the axle that toggle between active and passive states in response to acid or base. Trichloroacetic acid initiates the first stage of motion until it is decomposed by base in the solution, spurring the second phase. Science , this issue p. 340

Chlorotoxin (CLTX) is a neurotoxin found in the venom of the Israeli scorpion, Leirius quinquestriatus. It contains 36-amino acids with four disulfide bonds and inhibits low-conductance chloride channels. CLTX also binds to matrix metalloproteinase-2 (MMP-2) selectively. The synthesis of chlorotoxin using solid phase peptide synthesis (SPPS) is very difficult and has a very low yield (<1%) due to high number of amino acid sequence. In this work, to improve the efficiency of the synthesis, native chemical ligation was applied. In this strategy, chlorotoxin sequence was split into two parts having 15 and 21 amino acids. 21-mer peptide was synthesized in its native form based on 9-fluorenylmethyloxycarbonyl (Fmoc) chemistry. 15-mer peptide was synthesized having o-aminoanilide linker on C-terminal. These parts were coupled by native chemical ligation to produce chlorotoxin.