Stabilization challenges and aggregation in protein-based therapeutics in the pharmaceutical industry.

Protein-based therapeutics have revolutionized the pharmaceutical industry and become vital components in the development of future therapeutics. They offer several advantages over traditional small molecule drugs, including high affinity, potency and specificity, while demonstrating low toxicity and minimal adverse effects. However, the development and manufacturing processes of protein-based therapeutics presents challenges related to protein folding, purification, stability and immunogenicity that should be addressed.

Impact of ONU547 on the growth and acclimatization of micropropagated L. and Steud. plants to conditions.

Clonal micropropagation is an effective method for plant reproduction, applicable in both scientific and industrial domains. However, a significant number of microclones are lost during the acclimatization process. To address this, the introduction of beneficial microorganisms into the rhizosphere of micropropagated plants could have a positive effect on the survival rates and external characteristics of acclimatized plantlets.

Probiotic and technological characterization of selected Lactobacillus strains isolated from different egyptian cheeses.

Background: Fresh milk and natural environmental conditions are used to produce traditional cheeses. Such cheeses are produced by dozens of different types of microbes. Non-starter lactobacilli are the most responsible genus of lactic acid bacteria exhibiting key technological and health promoting traits.

Modulation of cytotoxic amyloid fibrillation and mitochondrial damage of α-synuclein by catechols mediated conformational changes.

The interplay between α-synuclein (α-syn) and catechols plays a central role in Parkinson's disease. This may be related to the modulating effects of catechols on the various aspects of α-syn fibrillization. Some of these effects may be attributed to the membrane-binding properties of the protein.

Bivalent metal ions induce formation of α-synuclein fibril polymorphs with different cytotoxicities.

α-Synuclein (α-Syn) aggregates are key components of intracellular inclusion bodies characteristic of Parkinson's disease (PD) and other synucleinopathies. Metal ions have been considered as the important etiological factors in PD since their interactions with α-Syn alter the kinetics of fibrillation. In the present study, we have systematically explored the effects of Zn, Cu, Ca, and Mg cations on α-Syn fibril formation.