N-(tert-butoxycarbonyl)-O-allyl-L-seryl-α-aminoisobutyryl-L-valine methyl ester: a protected tripeptide with an allylated serine residue.

The title compound [systematic name (6S,12S)-methyl 6-(allyloxymethyl)-12-isopropyl-2,2,9,9-tetramethyl-4,7,10-trioxo-3-oxa-5,8,11-triazatridecan-13-oate], C(21)H(37)N(3)O(7), containing the little studied O-allyl-L-serine residue [Ser(All)], crystallizes in the monoclinic space group C2 with one molecule in the asymmetric unit. The compound is an analogue of the Ser140-Val142 segment of the water channel aquaporin-4 (AQP4). It forms a distorted type-II β-turn with a P(II)-3(10L)-P(II) backbone conformation (P(II) is polyproline II).

N-(tert-butoxycarbonyl)-α-aminoisobutyryl-α-aminoisobutyric acid methyl ester: two polymorphic forms in the space group P2(1)/n.

The title compound (systematic name: methyl 2-{2-[(tert-butoxycarbonyl)amino]-2-methylpropanamido}-2-methylpropanoate), C(14)H(26)N(2)O(5), (I), crystallizes in the monoclinic space group P2(1)/n in two polymorphic forms, each with one molecule in the asymmetric unit. The molecular conformation is essentially the same in both polymorphs, with the α-aminoisobutyric acid (Aib) residues adopting ϕ and ψ values characteristic of α-helical and mixed 3(10)- and α-helical conformations. The helical handedness of the C-terminal residue (Aib2) is opposite to that of the N-terminal residue (Aib1).

N-(tert-butoxycarbonyl)-L-valyl-L-valine methyl ester: a twisted parallel β-sheet in the crystal structure of a protected dipeptide.

The title compound, C(16)H(30)N(2)O(5), crystallizes with three molecules in the asymmetric unit, each adopting a β-strand/polyproline II backbone conformation. The main-chain functional groups are hydrogen bonded into tapes having the characteristics of parallel β-sheets. Each tape has a left-handed twist and thus forms a helix, with six peptide molecules needed to complete a full 360° rotation.