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Effect of basic oligopeptides on the B‐Z transition of poly(dG‐dC)·poly(dG‐dC) in water–methanol solutions
Author(s) -
Votavová H.,
Pírková J.,
Gut V.,
Šponar J.,
Bláha K.
Publication year - 1991
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.360310303
Subject(s) - chemistry , enthalpy , trimer , tetramer , peptide , methanol , crystallography , monomer , transition temperature , circular dichroism , oligopeptide , stereochemistry , molecule , organic chemistry , thermodynamics , polymer , dimer , biochemistry , physics , superconductivity , quantum mechanics , enzyme
The effect of basic oligopeptides (Lys‐Ala‐Ala) n ( n = 1–5, 10) and (Lys‐Leu‐Ala) n ( n = 1–4) on the B‐Z transition of poly (dG‐dC)·poly (dG‐dC) in water–methanol solutions was investigated using CD and uv spectroscopy: In the absence of peptides, the concentration of methanol at the midpoint of the B‐Z transition is 64% at 25°C. The transition is temperature dependent and the B conformation is preferred at higher temperatures. All peptides tested shift the midpoint of the B‐Z transition to lower concentrations of methanol. For shorter peptides this effect increases with an increasing number of monomeric units, showing the importance of the number of positive charges in the peptide molecule. At conditions of low methanol content, the trimer and tetramer of the (Lys‐Leu‐Ala) n series have a greater effect on the B‐Z transition than the corresponding oligomers of the (Lys‐Ala‐Ala) n series. This indicates an important influence of the presence of hydrophobic groups in the peptide side chains on the binding. In the presence of peptides, the B‐Z transition is also temperature dependent and the B conformation is preferred at higher temperatures. The addition of peptides results in an increase of the transition midpoint and of the transition width. These parameters were used for the calculation of the transition enthalpy Δ H B‐Z in 65% methanol, which is −1.15 ± 0.25 kcal/base pair. Since the van't Hoff enthalpy Δ H VH calculated from the temperature dependence of the B‐Z transition in the absence of peptides is −130 kcal/mol, the length of the cooperative unit is about 110 base pairs. The results suggest that the mechanism of Z‐DNA induction is similar but not identical with that involved in the action of metal cations in aqueous solution.