Interfacial energy of polypeptide complex coacervates measured via capillary adhesion.

A systematic study of the interfacial energy (γ) of polypeptide complex coacervates in aqueous solution was performed using a surface forces apparatus (SFA). Poly(L-lysine hydrochloride) (PLys) and poly(L-glutamic acid sodium salt) (PGA) were investigated as a model pair of oppositely charged weak polyelectrolytes. These two synthetic polypeptides of natural amino acids have identical backbones and differ only in their charged side groups. All experiments were conducted using equal chain lengths of PLys and PGA in order to isolate and highlight effects of the interactions of the charged groups during complexation. Complex coacervates resulted from mixing very dilute aqueous salt solutions of PLys and PGA. Two phases in equilibrium evolved under the conditions used: a dense polymer-rich coacervate phase and a dilute polymer-deficient aqueous phase. Capillary adhesion, associated with a coacervate meniscus bridge between two mica surfaces, was measured upon the separation of the two surfaces. This adhesion enabled the determination of the γ at the aqueous/coacervate phase interface. Important experimental factors affecting these measurements were varied and are discussed, including the compression force (1.3-35.9 mN/m) and separation speed (2.4-33.2 nm/s). Physical parameters of the system, such as the salt concentration (100-600 mM) and polypeptide chain length (N = 30, 200, and 400) were also studied. The γ of these polypeptide coacervates was separately found to decrease with both increasing salt concentration and decreasing polypeptide chain length. In most of the above cases, γ measurements were found to be very low, <1 mJ/m(2). Biocompatible complex coacervates with low γ have a strong potential for applications in surface coatings, adhesives, and the encapsulation of a wide range of materials.