title: Thermodynamics of Ion Pair Formations Between Charged Poly(Amino Acid)s.
abstract: Electrostatic interactions between the positively and negatively charged amino acids in proteins play an important role in macromolecular stability, binding, and recognition. Numerous amino acids in proteins are ionizable and may exist in negatively (e.g., Glu, Asp, Cys, Tyr) or positively (e.g., Arg, Lys, His, Orn) charged form dependent on pH and their pKas. In this work, isothermal titration calorimetry was used to determine the average standard values of thermodynamic parameters (the Gibbs free energy, enthalpy, entropy, and the heat capacity) of interaction between the positively charged amino acid homopolymers (polyarginine, polylysine, and polyornithine) and the negatively charged homopolymers (polyaspartic and polyglutamic acids). These values are of potential use in the computational models of interacting proteins and other biological macromolecules. The study showed that oppositely charged poly(amino acid)s bound each other with the stoichiometry of one positive to one negative charge. Arginine bound to the negatively charged amino acids with exothermic enthalpy and higher affinity than lysine. This result also suggests that positive charges in proteins should not be considered entirely equivalent if carried by lysine or arginine. The difference in binding energy of arginine and lysine association with the negatively charged amino acids was attributed to the enthalpy of the second ionic hydrogen bond formation between the guanidine and carboxylic groups. Despite the favorable enthalpic contribution, all such ion pair formation reactions were largely entropy-driven. Consistent with previously observed ionic interactions, the positive heat capacity was always observed during the amino acid ion pair formation.
authors: Department of Biothermodynamics and Drug Design, Institute of Biotechnology, Vilnius University , V. A. Graičiu̅no 8, LT-02241 Vilnius, Lithuania.
authors: Vytautas
authors: V
authors: Petrauskas
authors: Department of Biothermodynamics and Drug Design, Institute of Biotechnology, Vilnius University , V. A. Graičiu̅no 8, LT-02241 Vilnius, Lithuania.
authors: Eglė
authors: E
authors: Maximowitsch
authors: Department of Biothermodynamics and Drug Design, Institute of Biotechnology, Vilnius University , V. A. Graičiu̅no 8, LT-02241 Vilnius, Lithuania.
authors: Daumantas
authors: D
authors: Matulis
mesh_terms: D019277:Entropy; D006860:Hydrogen Bonding; D008958:Models, Molecular; D010455:Peptides / Q000737:chemistry*; D011099:Polyglutamic Acid / Q000737:chemistry*; D011107:Polylysine / Q000737:chemistry*; D013816:Thermodynamics
chemical_list: D010455:Peptides; C008973:polyornithine; D011107:Polylysine; C015462:polyarginine; D011099:Polyglutamic Acid