Strel'tsov S A, Khorlin A A, Surovaia A N, Gurskiĭ G V, Zasedatelev A S
Biofizika. 1980 Sep-Oct;25(5):929-41.
The DNA binding activity of trivaline dansyl hydrazide was investigated by circular dichroism, UV spectrophotometry and fluorescence methods. It is shown that these peptides in the absence of DNA can adopt statistical coil and antiparallel beta-conformation and can exist in aqueous solution as monomers, dimers and higher orders aggregates depending upon the concentration and the presence of N- and C-blocking groups. The aggregation and disaggregation processes are very slow especially for N- and C-protected peptides. Our observations show that oligopeptides in the monomeric and dimeric forms bind to double-stranded DNA and RNA whereas tetramers and higher order aggregates exhibit no DNA binding activity. The binding of monomers is a cooperative process favoring the formation of deformed antiparallel beta-structure between adjacently bound monomers. The binding constant of dimeric oligovaline species to GC-rich DNA sequences is about 5 fold higher than that found from the binding of oligovaline to poly(dA) . poly(dT). The binding of dimers takes place in the minor DNA groove as revealed from our observations that oligovaline binds to T6 phage DNA containing massive glucose and diglucose residues in the major groove. The backbone C=0 groups of oligovaline probably serve as specific reaction centres for the interaction with guanine 2-amino groups in the minor DNA groove.