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The neuritic plaques formed by amyloid β-peptide (Aβ) play a seminal role in the pathogenesis of Alzheimer's disease (AD). Aβ sequence 25-35 (GSNKGAIIGLM) is among the most frequently studied Aβ derivatives for the reason that it possesses the structural characteristic of Aβ and remains neurotoxic. Aβ(25-35) was modified with an aliphatic chain (C 18 ) at the N-terminal of the peptide for the study of the Langmuir monolayer at the air-water interface. The main advantage of the 2D approach is the self-assembly of the peptide moiety in the subphase, and therefore the aggregation process of the peptidolipid Aβ(25-35) was monitored by surface pressure and surface potential-area isotherms. The real-time epifluorescence microscopy was utilized to observe the topography of the domains formed, whereas polarization modulation infrared reflection absorption spectroscopy (PM-IRRAS) provided the information on the structural features of the domains at the airwater interface. Langmuir-Blodgett films were prepared to examine by circular dichroism (CD) the conformation of the peptidolipid film in the domains.

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The growing discipline of proteomics is highly relevant in our quest to understand cause/effect relationships between environmental, Physiological, and pathological influences on bodily organ function. We present an overview of the principles and methods in profiling, functional, and structural proteomics and their applications to oncology and others related areas.