---

Research subject: Parkinson’s disease is a neurodegnerative disorder with no treatment due to the blood brain barrier (BBB) existence. The cure for this disease is Dopamine a chemical molecule.
Research approach: This study investigates biodegradable naoparticles (NPs) carrying dopamine (DA) across the blood–brain barrier. Ion polymerization and solvent methods were used to achieve this goal. Particle size, zeta potential, entrapment efficiency and in vitro drug release behavior, at pH 7 were examined.
Main results: The empty nanoparticles and drug-loaded nanoparticles were found to be spherical in shape and fluffy exterior, with mono-modal size distribution and negative zeta-potentials of increasing average sizes 90 to 120 nm simultaneously. Fourier transform infrared (FTIR) spectra demonstrated the polymerization of nBCA monomers and encapsulation of DA inside poly (butylcyanoacrylate) (PBCA).Thermal characteristics of the copolymer were investigated by Fourier-transform infrared spectroscopy (FTIR). Drug loading efficiency was around 25%.The in-vitro drug release profile of DA -loaded PBCA nanoparticles prepared from ion polymerization following solution techniques exhibited a gradual release; more than 20 ٪w/w of the drug was released after 51 h. The results showed that the DA–PBCA nanocapsules could be an effective carrier for hydrophilic agents. In this study, PBCA-NSPs were successfully generated as a delivery system for DA, providing a promising approach to improve the therapy of PDs.

 
 

---

Alpha-synuclein protein (α-syn) is the main factor known in Parkinson's disease. The expression of this protein has challenges. One of these challenges is the presence of protein in bacterial pellet. Studies have shown that the expression of proteins with tags such as small ubiquitin-like modifier (SUMO) increases the expression in the soluble phase, therefore the expression of α-syn with this sequence was investigated to increase the protein in the soluble phase. It has also been shown in studies that SUMOylation has an inhibitory effect on fibrillation, also in this study the effect of the SUMO on alpha-synuclein fibrillation was investigated. The α-syn gene was cloned with SUMO-tag. Nickel sepharose column was used to purify the protein, and dialysis was performed and fibrillation was checked by fluorescence emission of Thioflavin for 72 hours and was observed that the protein with SUMO sequence has a higher expression level, and 95% of the protein is in the soluble phase. On the other hand, it was shown that the SUMO sequence has an inhibitory effect on the process of amyloid fibril formation. The results obtained from previous studies showed that the binding of the SUMO sequence increases the expression and solubility of recombinant proteins. This study revealed that the presence of this sequence contributed to the protein expression level and the protein's presence in the solution phase. On the other hand, observations showed that this sequence has anti-fibrillation properties for proteins with amyloid properties, and in this study showed that SUMO prevents α-syn aggregation.