Scopus İndeksli Yayınlar Koleksiyonu / Scopus Indexed Publications Collection

Permanent URI for this collectionhttps://hdl.handle.net/11147/7148

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  • Article
    Citation - WoS: 6
    Citation - Scopus: 7
    Interface-Dependent Phononic and Optical Properties of Geo/Moso Heterostructures
    (Royal Society of Chemistry, 2022) Yağmurcukardeş, Mehmet; Sözen, Yiğit; Başkurt, Mehmet; Peeters, François M.; Şahin, Hasan
    The interface-dependent electronic, vibrational, piezoelectric, and optical properties of van der Waals heterobilayers, formed by buckled GeO (b-GeO) and Janus MoSO structures, are investigated by means of first-principles calculations. The electronic band dispersions show that O/Ge and S/O interface formations result in a type-II band alignment with direct and indirect band gaps, respectively. In contrast, O/O and S/Ge interfaces give rise to the formation of a type-I band alignment with an indirect band gap. By considering the Bethe-Salpeter equation (BSE) on top of G0W0 approximation, it is shown that different interfaces can be distinguished from each other by means of the optical absorption spectra as a consequence of the band alignments. Additionally, the low-and high-frequency regimes of the Raman spectra are also different for each interface type. The alignment of the individual dipoles, which is interface-dependent, either weakens or strengthens the net dipole of the heterobilayers and results in tunable piezoelectric coefficients. The results indicate that the possible heterobilayers of b-GeO/MoSO asymmetric structures possess various electronic, optical, and piezoelectric properties arising from the different interface formations and can be distinguished by means of various spectroscopic techniques.
  • Article
    Citation - WoS: 100
    Citation - Scopus: 97
    Novel Trimodal Maldi Imaging Mass Spectrometry (ims3) at 10 Μm Reveals Spatial Lipid and Peptide Correlates Implicated in Aß Plaque Pathology in Alzheimer's Disease
    (American Chemical Society, 2017) Kaya, İbrahim; Brinet, Dimitri; Michno, Wojciech; Başkurt, Mehmet; Zetterberg, Henrik; Blenow, Kaj; Hanrieder, Jo¨rg
    Multimodal chemical imaging using matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS) can provide comprehensive molecular information in situ within the same tissue sections. This is of relevance for studying different brain pathologies such as Alzheimer's disease (AD), where recent data suggest a critical relevance of colocalizing Aβ peptides and neuronal lipids. We here developed a novel trimodal, high-resolution (10 μm) MALDI imaging MS (IMS) paradigm for negative and positive ion mode lipid analysis and subsequent protein ion imaging on the same tissue section. Matrix sublimation of 1,5-diaminonaphthalene (1,5-DAN) enabled dual polarity lipid MALDI IMS on the same pixel points at high spatial resolutions (10 μm) and with high spectral quality. This was followed by 10 μm resolution protein imaging on the same measurement area, which allowed correlation of lipid signals with protein distribution patterns within distinct cerebellar regions in mouse brain. The demonstrated trimodal imaging strategy (IMS3) was further shown to be an efficient approach for simultaneously probing Aβ plaque-associated lipids and Aβ peptides within the hippocampus of 18 month-old transgenic AD mice (tgArcSwe). Here, IMS3 revealed a strong colocalization of distinct lipid species including ceramides, phosphatidylinositols, sulfatides (Cer 18:0, PI 38:4, ST 24:0) and lysophosphatidylcholines (LPC 16:0, LPC 18:0) with plaque-associated Aβ isoforms (Aβ 1-37, Aβ 1-38, Aβ 1-40). This highlights the potential of IMS3 as an alternative, superior approach to consecutively performed immuno-based Aβ staining strategies. Furthermore, the IMS3 workflow allowed for multimodal in situ MS/MS analysis of both lipids and Aβ peptides. Altogether, the here presented IMS3 approach shows great potential for comprehensive, high-resolution molecular analysis of histological features at cellular length scales with high chemical specificity. It therefore represents a powerful approach for probing the complex molecular pathology of, e.g., neurodegenerative diseases that are characterized by neurotoxic protein aggregation.