Investigations into the interaction thermodynamics of TRAP-related peptides with a temperature-responsive polymer-bonded porous silica stationary phase

The interaction thermodynamics of the thrombin receptor agonistic peptide (TRAP-1), H-Ser-Phe-Leu-Leu-Arg-Asn-Pro-OH, and a set of alanine scan substitution peptides, have been investigated with an n -octadecylacrylic polymer-bonded porous silica (Sil-ODA 18 ) and water-acetonitrile mobile phases at temperatures ranging from 5 to 80 °C in 5 °C increments. The retention of these peptides on the Sil-ODA 18 stationary phase decreased as the water content in the mobile phase was lowered from 80% (v/v) to ca . 45% (v/v) and reached a minimum value for each peptide at a specific water-acetonitrile composition. Further decreases in the water content of the mobile phase led to increased retention. The magnitude of the changes in enthalpy of interaction, Δ H a s s o c 0 , changes in entropy of interaction, Δ S a s s o c 0 , and changes in heat capacity, Δ C p 0 , were found to be dependent on the molecular properties of the mobile phase, the temperature, the structure/mobility of the stationary phase, and the conformation and solvation state of the peptides. With water-rich mobile phases, the retention behaviour of the TRAP analogues was dominated by enthalpic processes, consistent with the participation of strong hydrogen bonding effects, but became dominated by entropic effects with acetonitrile-rich mobile phases as the temperature was increased. These changes in the retention behaviour of these TRAP peptides are consistent with the generation of water or acetonitrile clusters in the mobile phase depending on the volume fractions of the organic solvent as the Sil-ODA 18 stationary phase transitions from its crystalline to its isotropic state. Image 1 • Selectivity profiles of a multi-responsive adsorbent have been evaluated. • TRAP-related synthetic peptide analogues have been used as analytes. • Isocratic elution analyses performed at different temperature, T , conditions. • Phase structure changed from crystalline to isotropic in response to T change. • Thermodynamic parameters of peptide interaction derived from van't Hoff plots.