Interaction between amyloid beta peptide and an aggregation blocker peptide mimicking islet amyloid polypeptide.

Autor: Nasrollah Rezaei-Ghaleh, Erika Andreetto, Li-Mei Yan, Aphrodite Kapurniotu, Markus Zweckstetter

Publikováno v: PLoS ONE, Vol 6, Iss 5, p e20289 (2011)

Assembly of amyloid-beta peptide (Aβ) into cytotoxic oligomeric and fibrillar aggregates is believed to be a major pathologic event in Alzheimer's disease (AD) and interfering with Aβ aggregation is an important strategy in the development of novel

Externí odkaz: https://doaj.org/article/19dab0f40007472e8c5fa4c803f69293

Guided folding takes a start from the molecular imprinting of structured epitopes

Autor: Graziano Guella, Erika Andreetto, Alessandra Bossi, Andrea Anesi, Emmanuele Ambrosi, Lucia Cenci

Publikováno v: Nanoscale. 8:15665-15670

A biomimetic route towards assisted folding was explored. Molecularly imprinted polymeric nanoparticles (MIP NPs), i.e. biomimetics with entailed molecular recognition properties made by a template assisted synthesis, were prepared to target a struct

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dabfdd7c0b2ad4d0488399ea61a1bf2e
https://doi.org/10.1039/c6nr03467e

A Hot‐Segment‐Based Approach for the Design of Cross‐Amyloid Interaction Surface Mimics as Inhibitors of Amyloid Self‐Assembly

Autor: Eleni Malideli, Andrea Caporale, Michael Kracklauer, Karine Farbiarz, Erika Andreetto, Anna Spanopoulou, Tatjana Neumüller, Aphrodite Kapurniotu, Li-Mei Yan, Bernd Reif, Maria Bakou, Gerhard Rammes, Marianna Tatarek-Nossol, Elke Prade

Publikováno v: Angewandte Chemie (Int. ed., Print) 54 (2015): 13095–13100. doi:10.1002/anie.201504973
info:cnr-pdr/source/autori:Andreetto, Erika; Malideli, Eleni; Yan, Li-Mei; Kracklauer, Michael; Farbiarz, Karine; Tatarek-Nossol, Marianna; Rammes, Gerhard; Prade, Elke; Neumueller, Tatjana; Caporale, Andrea; Spanopoulou, Anna; Bakou, Maria; Reif, Bernd; Kapurniotu, Aphrodite/titolo:A Hot-Segment-Based Approach for the Design of Cross-Amyloid Interaction Surface Mimics as Inhibitors of Amyloid Self-Assembly/doi:10.1002%2Fanie.201504973/rivista:Angewandte Chemie (Int. ed., Print)/anno:2015/pagina_da:13095/pagina_a:13100/intervallo_pagine:13095–13100/volume:54

The design of inhibitors of protein-protein interactions mediating amyloid self-assembly is a major challenge mainly due to the dynamic nature of the involved structures and interfaces. Interactions of amyloidogenic polypeptides with other proteins a

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::101355da42e807627e1fd77e2a12e3a1
https://doi.org/10.1002/anie.201504973

Screening of the binding properties of molecularly imprinted nanoparticles via capillary electrophoresis

Autor: Giacomo Musile, Emmanuele Ambrosi, Lucia Cenci, Erika Andreetto, Alessandra Bossi, Franco Tagliaro

In response to the need for straightforward analytical methods to assess the affinity of molecularly imprinted nanoparticles (MIP NPs) for ligands, capillary electrophoresis (CE) was exploited using MIP NPs targeting the iron-regulating hormone hepci

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f09624385dfbc7c3016bd47201d0052b
http://hdl.handle.net/11562/938538

Amyloid-Kreuzwechselwirkung zur Inhibierung der Proteinaggregation, nicht aber der Proteinfunktion: Inhibierung der Insulinaggregation im nanomolaren Bereich durch ein IAPP-Mimetikum

Autor: Marianna Tatarek-Nossol, Aphrodite Kapurniotu, Aleksandra Velkova, Erika Andreetto

Publikováno v: Angewandte Chemie. 120:7222-7227

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::e0f5413fed1e043bd123cae62aa1c35c
https://doi.org/10.1002/ange.200801499