Conformations of spermine in adenosine triphosphate complex: The structural basis for weak bimolecular interactions of major cellular electrolytes

Selectively ²H- and ¹³C-labeled spermines (SPM) were efficiently synthesized and analyzed by NMR spectroscopy to determine the spin-spin coupling constants for six conformationally relevant bonds. SPM that is composed of three alkyl moieties, a butanylene, and two propanylene chains undergoes a conformational change when interacting with multivalent anions (e.g., adenosine triphosphate (ATP), ATP-Mg²⁺, and tripolyphosphate). Upon interaction with ATP, the C-C bonds, which affect the distance between the neighboring pairs of ammonium groups (i.e., N1/N5 and N5/N5′), increase the population of gauche rotamers by 17-20 % relative to those in the 4 HCl salt of SPM. However, the trend in increments of the gauche conformers for the SPM-ATP complex profoundly differs from that of the spermidine (SPD)-ATP complex. This implies that SPM may preferentially recognize the adenyl group of ATP rather than the tripolyphosphate moiety. This may account for the higher affinity of SPM to ATP-Mg²⁺ than with that of SPD, which chiefly interacts with β- and Î-phosphates and is easily replaced by Mg ²⁺. These results may provide a clue for the further understanding of the structural basis of polyamine biological functions. Spermines and spin: Spermines (SPM) labeled selectively with ²H and ¹³C were used to determine the spin-spin coupling constants for six conformationally relevant bonds. SPM revealed diverse conformational changes upon interaction with adenosine triphosphate (ATP), ATP-Mg²⁺, and tripolyphosphate (TPP, see graph).