Poly(8-aminoguanylic acid): formation of ordered self-structures and interaction with poly(cytidylic acid)

Biochemistry. 1975 Nov 18;14(23):5033-45. doi: 10.1021/bi00694a002.

Abstract

Poly(8-aminoguanylic acid) has in neutral solution a novel ordered structure of high stability. The 8-amino group permits formation of three hydrogen bonds between two residues along the "top", or long axis, of the purines. The usual hydrogen bonding protons and Watson-Crick pairing sites are not involved in the association. The bonding scheme has a twofold rotation axis and is hemiprotonated at N(7). Poly(8NH2G) is converted by alkaline titration (pK = 9.7) to a quite different ordered structure, which is the favored form over the range approximately pH 10-11. The bonding scheme appears to be composed of a planar, tetrameric array of guanine residues, in which the 8-amino group does not participate in interbase hydrogen bonding. Poly (8NH2G) does not interact with poly(C) in neutral solution because of the high stability of the hemiprotonated G-G self-structure. Titration to the alkaline plateau, however, permits ready formation of a two-stranded Watson-Crick helix. In contrast to the monomer 8NH2GMP, poly(8NH2G) does not form a triple helix with poly(C) under any conditions. The properties of the ordered structures are interpreted in terms of a strong tendency of the 8-amino group to form a third interbase hydrogen bond, when this possibility is not prevented by high pH.

MeSH terms

  • Binding Sites
  • Circular Dichroism
  • Drug Stability
  • Escherichia coli / enzymology
  • Hydrogen Bonding
  • Hydrogen-Ion Concentration
  • Micrococcus / enzymology
  • Models, Molecular
  • Nucleic Acid Conformation
  • Poly C*
  • Poly G / analogs & derivatives*
  • Polyribonucleotide Nucleotidyltransferase / metabolism
  • Polyribonucleotides* / analogs & derivatives*
  • Spectrophotometry, Infrared
  • Spectrophotometry, Ultraviolet
  • Temperature

Substances

  • Polyribonucleotides
  • Poly G
  • Poly C
  • Polyribonucleotide Nucleotidyltransferase