Folding of the Squash Trypsin Inhibitor EETI II

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Abstract
A peptide, corresponding to the entire sequence of the squash trypsin inhibitor EETI II (Ecballium elaterium trypsin inhibitor) in which the six cysteines, engaged in three disulphide bridges in native EETI II, have been replaced by six serines, has been synthesised. CD, Fourier‐transform infrared spectroscopy (FTIR) and 1H‐NMR studies of this peptide revealed that some secondary structures present in native EETI II are still populated in the absence of disulphide bonds. Native‐like secondary structures were observed for segments 10–15 (helix), 16–19 and 22–25 (reverse turns) but no native tertiary interaction was detected. However, a non‐native local interaction between the aromatic ring of Phe26 and the amide group of Gly28 was observed. It is hypothesised that the 10–15, 16–19 and 22–25 native‐like local conformations could play a major role in the early folding of EETI II.

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