Self-assembling of poly(aspartic acid) with bovine serum albumin in aqueous solutions

• Published in: International journal of biological macromolecules Vol. 95; pp. 412 - 420
• Main Authors: Nita, L.E., Chiriac, A.P., Bercea, M., Asandulesa, M., Wolf, Bernhard A.
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 01.02.2017
• Subjects: Animals; Bovine serum albumin; Cattle; Hydrogen-Ion Concentration; Interpolymer complex; Models, Molecular; Peptides - chemistry; Poly(aspartic acid); Protein Binding; Protein Conformation; Self-assembling; Serum Albumin, Bovine - chemistry; Solutions; Water - chemistry; Bovine serum albumin; Poly(aspartic acid); Interpolymer complex; Self-assembling
• ISSN: 0141-8130; 1879-0003
• DOI: 10.1016/j.ijbiomac.2016.11.080

[Display omitted] Formation of PPCs by self-assembling between PAS and BSA as function of the PAS/BSA molar ratio (x*). Macromolecular co-assemblies built up in aqueous solutions, by using a linear polypeptide, poly(aspartic acid) (PAS), and a globular protein, bovine serum albumin (BSA), have been studied. The main interest was to identify the optimum conditions for an interpenetrated complex formation in order to design materials suitable for biomedical applications, such as drug delivery systems. BSA surface possesses several amino- and carboxylic groups available for covalent modification, and/or bioactive substances attachment. In the present study, mixtures between PAS and BSA were investigated at 37°C in dilute aqueous solution by viscometry, dynamic light scattering and zeta potential determination, as well as in solid state by AFM microscopy and dielectric spectroscopy. The experimental data have shown that the interpolymer complex formation occurs for a PAS/BSA molar ratio around 0.541.