Advances in Amyloid Aggregation and Its Inhibition: Implementing Insights from Physiological Conditions
A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Molecular Neurobiology".
Deadline for manuscript submissions: 28 February 2026 | Viewed by 2127
Special Issue Editor
Special Issue Information
Dear Colleagues,
Protein aggregation is linked with multiple life-worsening conditions collectively known as neurodegenerative diseases and amyloidosis. Currently there are only a few disease-modifying drugs approved, and a portion of them introduce severe side effects, suggesting the need to expand and improve further studies in the field. Initially the protein aggregation and drug screening are investigated under in vitro conditions, which provide faster and cheaper primary insights about protein misfolding. However, the in vitro results often tend to mismatch the findings in vivo—different aggregation pathways, formed fibril structures and the effects of inhibiting molecules. A corresponding difference is probable due to missing physiological conditions, including interacting molecules, molecular crowding, and ionic strength.
In this Special Issue for IJMS, we will focus on protein aggregation and inhibition studies at closer physiological conditions. We also welcome original articles, reviews that show potential protein aggregation modulators in vitro and in cells, improved aggregation protocols and comparrisons of protein fibrillation between in vitro and physiological conditions.
Dr. Andrius Sakalauskas
Guest Editor
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Keywords
- protein aggregation
- amyloid
- physiological conditions
- aggregation inhibition
- neurodegenerative diseases
- amyloidosis
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