UNIVERSITY OF BUCHAREST
FACULTY OF PHYSICS

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2026-06-11 23:58
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Conference: Bucharest University Faculty of Physics 2026 Meeting


Section: Biophysics; Medical Physics


Title:
Amyloid-Like Bovine Serum Albumin Fibrils as Protein Scaffold for Biointerfaces


Authors:
Jessica-Naomi ANGHELACHE (1), Any Cristina SERGENTU (2,3), Claudia CHILOM (1), Andrei NIȚESCU (2), Liviu NEDELCU (2), Teodor Adrian ENACHE (2,4)


*
Affiliation:
1) Faculty of Physics, University of Bucharest, 077125 Magurele, Ilfov, Romania

2) National Institute of Materials Physics, 405A Atomistilor Str., 077125 Magurele, Romania

3) Faculty of Materials Science and Engineering, National University of Science and

Technology POLITEHNICA Bucharest, Splaiul Independentei 313, 060042 Bucharest,

Romania

4) CIFRA- Centre International de Formation et de Recherche Avancées en Physique, 409,

Atomistilor Str., 077125, Măgurele, Romania


E-mail
jessica-naomi.anghelache@s.unibuc.ro adrian.enache@infim.ro


Keywords:
Amyloid fibrils, BSA, Supramolecular assembly, AFM, Biointerfaces


Abstract:
Amyloid-like protein assemblies represent a class of supramolecular systems with well- defined structural transitions and emergent physicochemical properties, making them attractive for biointerface engineering. In this work, the controlled fibrillation of bovine serum albumin (BSA) and the resulting structure-function relationships were investigated from a bio- physicochemical perspective. The initial conformational stability of BSA in different media was assessed by UV-Vis spectroscopy, confirming the preservation of native-like structural features prior to fibrillation. Amyloid-like conversion was induced under acidic and thermal conditions (pH 2, 65 °C), enabling a reproducible transition toward ordered aggregates. Fourier Transform Infrared Spectroscopy (FTIR) spectroscopy revealed a progressive decrease in α-helical content accompanied by the emergence of β-sheet-rich structures, consistent with nucleation-dependent fibrillation mechanisms. The kinetics and extent of fibril formation were further supported by Thioflavin T fluorescence, indicating the development of extended cross-β architectures. Atomic Force Microscopy (AFM) provided direct morphological evidence of the hierarchical assembly process, highlighting the transition from globular intermediates to elongated fibrillar networks. Notably, ionic strength was found to modulate fibril organization, with salt-containing environments promoting lateral association and the formation of interconnected supramolecular networks, suggesting electrostatic screening effects governing intermolecular interactions. At the biointerface level, fibril-coated substrates were evaluated using SH-SY5Y neuronal- like cells. The results demonstrated that the nanoscale topography and structural organization of the fibrils significantly influence cell adhesion and spreading, indicating a strong coupling between supramolecular architecture and cellular response. Overall, this study provides insight into the physicochemical mechanisms underlying BSA fibrillation and highlights the role of environmental parameters in tuning fibrillar organization. These findings support the use of amyloid-like protein assemblies as tunable platforms for engineering functional biointerfaces with controlled structural and interfacial properties.


References:

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Acknowledgement:
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