Circular dichroism of poly(β-benzyl-l-aspartate) films in the α, β and ω conformations

The conformations of poly(β-benzyl l-aspartate) (PBLA) in film were studied by means of circular dichroism (c.d.). Films of PBLA show c.d. which is related to the benzyl chromophores of this polypeptide. The magnitude and sign of the c.d. of the benzyl chromophores depend on the conformation i.e. α-helix, ω-helix or β-form. The aromatic c.d. of the left-handed α-helix or the left-handed ω-helix is negative in sign, and that of the β-form is positive in sign. The absolute magnitude of the c.d. of PBLA is much larger in the ω-helical conformation than in the α-helical or the β-conformations. In the left-handed α-helical PBLA (α-PBLA), the positive dichroism band of the $\text{n?π1}$ peptide electronic transition is observed at about 226 nm. When the α-PBLA is converted to the left-handed ω-helical PBLA (ω-PBLA), the band at 226 nm shifts to 224 nm, and its magnitude becomes much smaller. In the β-form PBLA (β-PBLA), this band is negative in sign and observed at 223 nm. The absolute magnitude of the c.d. relative to this electronic transition follows the order: β-form < ω-helix < α-helix.