SearcharxivSearch

arXiv subjects

Lech Tomasz Baczewski

Publications and source records attributed to Lech Tomasz Baczewski.

2 recordsLinked to original sources

Microscopic and macroscopic characterization: MBE-grown versus sputter-deposited Au/Co/Au thin films for CISS and MIPAC effect studies

Chirality-induced spin selectivity (CISS) enables spin-dependent transport at chiral molecule/Au(111) interfaces and is used in spintronics when combined with ferromagnetic thin films in spin-valve-type hybrids. However, the influence of substrate microstructure on CISS and the related magnetization induced by the proximity of adsorbed chiral molecules (MIPAC) effect is still not well understood. In this study, we compare the effects of the adsorption of L-chiral alpha-helical alanine-rich peptides on Au/Co/Au ferromagnetic thin films fabricated by molecular beam epitaxy (MBE) and magnetron sputtering. X-ray reflectivity and X-ray diffraction show sharper interfaces and a narrower Au(111) rocking-curve width for the MBE-grown sample. However, atomic force microscopy and scanning tunneling microscopy images reveal that both sample types have locally smooth Au(111) surface regions suitable for peptide adsorption, despite clear differences in larger-scale morphology. Microscopic scanning tunneling spectroscopy after peptide exposure yields similar magnetization-direction-dependent tunneling currents in both sample types, confirming a similar magnitude CISS effect on the molecular scale. In contrast, macroscopic magneto-optical Kerr effect hysteresis loops and effect microscopy reveals that only sputter-deposited samples show slight coercivity enhancements and a consistent reduction in domain wall velocity after peptide exposure. These results suggest that microscopic CISS signatures are robust for both sample types, whereas macroscopic MIPAC-type magnetic responses are more sensitive to the substrate microstructure.

cond-mat.mtrl-sci

Spin-Dependent Amyloid Self-Assembly on Magnetic Substrates

Protein aggregation into insoluble amyloid-like fibrils is implicated in a wide range of diseases and understanding its nucleation process is a key for mechanistic insights and advancing therapeutics. The electronic charge of the amyloidogenic monomers significantly influences their self-assembly process. However, the impact of electron spin interactions between monomers on amyloid nucleation has not been considered yet. Here, we studied amyloid formation on magnetic substrates using Scanning Electron Microscopy (SEM), fluorescence microscopy, and Attenuated Total Reflection Fourier Transform Infrared (ATR-FTIR) Spectroscopy. We observed a preferred magnetization orientation of the ferromagnetic layer for fibril formation, leading to twice as many and significantly longer fibrils (up to 20 times) compared to the opposite magnetization orientation. This preference is related to monomer chirality. Additionally, fibril structure varied with substrate magnetization orientation. Our findings suggest a transient spin polarization in monomers during self-assembly, driven by the Chiral Induced Spin Selectivity (CISS) effect. These effects are consistent for various molecule length scales, from A-beta polypeptide to dipeptides and single amino acids, indicating a fundamental spin-based dependence on biomolecular aggregation that could be applied in novel therapeutic interventions targeted for amyloid-related diseases.

physics.chem-ph