Background: Charge and hydrophobicity are key factors for the construction of bioactive proteins on bio-substrates. Amyloid-beta (Aβ) is a biomarker of Alzheimer's disease and cerebral amyloid angiopathy, and this study explores its multi-faceted bioactivity guided by bio-substrates. Methods: Initially, the dynamic mode was used to confirm the homemade rhAβ42, and then bio-substrates and metal ions were screened to construct rhAβ42 oligomers. In the static mode, hydrophobicity and morphology were analyzed through contact angle and microscopy, and WST-1 was used to investigate the bioactivity of monomers and oligomers constructed on bio-substrates. Significant findings: The results show that the homemade rhAβ42 and rhAβ-Cu oligomers are not only recognized by specific antibodies, but also Protein G and Type B gelatin combined with ferric were constructed as rhAβ-Fe oligomers in this dynamic model. Static pattern analysis indicates that Type B gelatin had the relatively highest hydrophobicity and directly affects rhAβ42 binding. Morphologically, Protein G and Type B gelatin are used as bio-substrates to construct two-dimensional leaf vein-like and three-dimensional columnar structures, and there is a clear difference between 10 % promotion and 70 % mortality at different bioactive profiles. We hope to contribute to the cerebral amyloid angiopathy-related research and in vitro pathogenic microenvironmental models in the future.
Date:
2024-10
Relation:
Journal of the Taiwan Institute of Chemical Engineers. 2024 Oct;163:Article number 105570.
