The serum albumin has been used as a drug nanocarrier for a long time due to its rich drug transportation ability. Here, modified bovine serum albumin (BSA) proteins were obtained by conjugation with ethylenediamine and dopamine molecules, separately. Using these modified proteins, new BSA nanoparticles were obtained by a desolvation method. Native BSA has a net negative charge at the physiological condition. However, ethylenediamine conjugation yields a positive charge on it, and thus produces cationic BSA (cBSA) protein. On the other hand, dopamine functionalization (D-BSA) makes BSA eager to coordinate with transition metals. After preparation of modified proteins (cBSA and D-BSA), their nanoparticles were prepared with desolvation method but using different crosslinking mechanisms. For cBSA NPs preparation, a traditional crosslinking agent of glutaraldehyde was used. However, for D-BSA NPs preparation, Fe(III) ions were added to the system to achieve the stable nanoparticle formation. In order to obtain cBSA NPs, several organic solvents were used as desolvating agents. cBSA NPs with an average size around 200 nm were obtained in a high formation yield (54.8%) only through addition of acetonitrile to the cBSA aqueous solution. Similarly, different desolvating agents were studied to obtain D-BSA NPs. The promising results were obtained upon addition of 1:5 (v/v) of water/acetone mixture. After addition of the desolvating agent, Fe(III) ions were added to the solution to interconnect D-BSA with each other. This connection is pH sensitive therefore albumin nanoparticles were stable at basic pH values but not at acidic pH values. By this way, pH sensitive D-BSA NPs around 300 nm particle sizes were obtained.