Abstract
The crystal structure of the pentapeptide p-toluene-sulfonyl-(α-aminoisobutyryl) 5-methyl ester (Tosyl-(Aib) 5-OMe) has been determined in the space group P I . Pentapeptide molecules are folded in the 3 10 helical conformation and packed together, so as to yield a hydrophobic channel with a minimim diameter of 5.2 Å. The channel contains crystallographically disordered material. This structure provides a model for channel formation by hydrophobic peptide aggregates and should prove useful in studies of alamethicin, suzukacillin and related Aib containing membrane channels. Triclinic (P I ) crystals of the pentapeptide are obtained in the presence of LiClO 4 in aqueous methanol, whereas crystallization from methanol alone yields crystals in the space group Pbca. The conformations of the peptide in the two crystal forms are very similar and only the molecular packing is dramatically different.
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