abstract background antibiotic resistance makes antimicrobial peptides (amps) agents an alternative for treatment of pathogenic diseases. they are isolated from various animals invertebrates, vertebrates and plants. the present study shows the electrophoretic pattern of protein and peptides from vicia faba seed and reports our first attempt to study the antibacterial activity of vicia faba seed...

Alzheimer's disease is most common neurodegenerative disorder and is characterized by increased production of soluble amyloid-β oligomers, the main toxic species predominantly formed from aggregation of monomeric amyloid-β (Aβ). Increased production of Aβ invokes a cascade of oxidative damages to neurons and eventually leads to neuronal death. This study was aimed to investigate the neuroprotec...

We have previously developed a linker technology for half-life extension of peptides, proteins and small molecule drugs (1). The linkers undergo β-elimination reactions with predictable cleavage rates to release the native drug. Here we utilize this technology for half-life extension of the 38 amino acid HIV-1 fusion inhibitor TRI-1144. Conjugation of TRI-1144 to 40 kDa PEG by an appropriate β-...

The membrane bound metalloprotease meprin β is important for collagen fibril assembly in connective tissue formation and for the detachment of the intestinal mucus layer for proper barrier function. Recent proteomic studies revealed dozens of putative new substrates of meprin β, including the amyloid precursor protein (APP). It was shown that APP is cleaved by meprin β in distinct ways, either ...

Amyloid-β (Aβ) peptide deposition, hyperphosphorylated tau proteins, reactive astrocytes, high levels of metal ions, and upregulated monoamine oxidases are considered to be the primary pathological markers Alzheimer’s disease (AD). Among them, Aβ deposition or plaques, is regarded as initial factor in pathogenesis AD a critical hallmark AD. This review highlights recently Aβ-specific fluorescen...

The 16–22 amino acid fragment of the β-amyloid peptide associated with the Alzheimer’s disease, Aβ, is capable of forming amyloid fibrils. Here we study the aggregation mechanism of Aβ16−22 peptides by unbiased thermodynamic simulations at the atomic level for systems of one, three and six Aβ16−22 peptides. We find that the isolated Aβ16−22 peptide is mainly a random coil in the sense that both...

Signal-peptide-mediated ER localization of mRNAs encoding for membrane and secreted proteins, and RNA-zipcode-mediated intracellular targeting of mRNAs encoding for cytosolic proteins are two well-known mechanisms for mRNA localization. Here, we report a previously unidentified mechanism by which mRNA encoding for Dia1, a cytosolic protein without the signal peptide, is localized to the perinuc...

The 16–22 amino acid fragment of the β-amyloid peptide associated with the Alzheimer’s disease, Aβ, is capable of forming amyloid fibrils. Here we study the aggregation mechanism of Aβ16−22 peptides by unbiased thermodynamic simulations at the atomic level for systems of one, three and six Aβ16−22 peptides. We find that the isolated Aβ16−22 peptide is mainly a random coil in the sense that both...