Influence of PEGylation on the ability of carboxymethyl-dextran to form complexes with α-lactalbumin

•Poly(ethylene glycol) was attached to reducing end of carboxymethyl-dextran (CMD).•Protein complex formation occurred at pH 5.9 for PEGylated CMD vs. pH 5.5 for CMD.•Phase separation of complexes not influenced by amount of PEGylated CMD.•Spheroidal complexes possessed hydrodynamic radius of 11–40 nm.

Electrostatic interactions between α-lactalbumin (α-lac) and carboxymethyldextran (CMD) in acidic solutions lead to phase-separated complexes. By adding a non-ionic poly(ethylene glycol) (PEG) chain onto the reducing end of CMD, forming carboxymethyl-dextran-block-poly(ethylene glycol) (CMD-b-PEG), the PEG block was hypothesized to reduce interactions with α-lac and promote formation of a micelle-like complex structure. Formation of complexes between α-lac and CMD-b-PEG or α-lac and CMD was determined following acidification by light scattering and electrophoretic mobility. Phase separation, size, and structure of α-lac/CMD-b-PEG complexes were characterized by turbidimetry, dynamic light scattering, and electron microscopy, respectively. Complexes of α-lac/CMD-b-PEG formed at pH values near pH 6, while α-lac/CMD complexes formed at pH 5.5. Both CMD and CMD-b-PEG decreased the charge of α-lac below pH 5.5 and led to phase separation below pH 5. Shift in charge and the critical pH of phase separation were both sensitive to the α-lac to CMD ratio, while the relative amount of CMD-b-PEG did not significantly influence either. Hydrodynamic radii of α-lac/CMD-b-PEG complexes was between 11 and 20 nm, which increased with increasing α-lac to CMD-b-PEG ratio and with decreasing pH. Spheroidal structures of ∼10 nm were also observed in micrographs that were attributed to α-lac/CMD-b-PEG complexes.