Strategy to discover full-length amyloid-beta peptide ligands using high-efficiency microarray technology
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Strategy to discover full-length amyloid-beta peptide ligands using high-efficiency microarray technology
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513 views
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Galati C, Spinella N, Renna L, Milardi D, Attanasio F, Sciacca MFM, Bongiorno C
Beilstein J Nanotech (ISSN: 2190-4286)
,
2017 Nov 20;
8(1): 2446-2453.
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Paper type:
Journal Article,
Impact factor:
2.968,
5-year impact factor:
3.191
Url:
https://www.scopus.com/inward/record.uri?eid=2-s2.0-85037535994&doi=10.3762%2fbjnano.8.243&partnerID=40&md5=2644aed5b25fd9e5ef545f91aada13f0
Keywords:
Alzheimer, S Disease, Tem, Florescence, High Sensitivity, Peptide, Silicon Oxide, Bins, Bioassay, Efficiency, Glycoproteins, High Resolution Transmission Electron Microscopy, Microarrays, Neurodegenerative Diseases, Amyloid-Beta Peptides, Experimental Investigations, Fibrillar Aggregates, Intermediate Structures, Microarray Technologies,
Affiliations:
*** IBB - CNR ***
STMicroelectronics, Stradale Primosole, 95121, Catania, Italy., CNR-Istituto di Biostrutture e Bioimmagini, Catania, Italy., IMM-CNR, Catania, Italy.,
References:
Not available.
Strategy to discover full-length amyloid-beta peptide ligands using high-efficiency microarray technology
Although the formation of β-amyloid (Aβ) fibrils in neuronal tissues is a hallmark of Alzheimer disease (AD), small-sized Aβ oligomers rather than mature fibrils have been identified as the most neurotoxic species. Therefore, the design of new inhibitors, able to prevent the aggregation of Aβ, is believed to be a promising therapeutic approach to AD. Unfortunately, the short-lived intermediate structures that occur in a solution along the Aβ aggregation pathway escape conventional experimental investigations and there is urgent need of new tools aimed at the discovery of agents targeting monomeric Aβ and blocking the early steps of amyloid aggregation. Here, we show the combination of high-efficiency slides (HESs) with peptide microarrays as a promising tool for identifying small peptides that bind Aβ monomers. To this aim, HESs with two immobilized reference peptides, (i.e., KLVFF and Semax) with opposite behavior, were investigated for binding to fluorescently labeled Aβ peptide. Transmission electron microscopy was used to demonstrate Aβ fibrillar aggregates missing. The use of HESs was critical to ensure convenient output of the fluorescent microarrays. The resulting sensitivity, as well as the low sample consumption and the high potential for miniaturization, suggests that the proposed combination of peptide microarrays and highly efficient slides would be a very effective technology for molecule profiling in AD drug discovery. © 2017 Galati et al.
Strategy to discover full-length amyloid-beta peptide ligands using high-efficiency microarray technology
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Galectins: Structure, function and therapeutic potential inhibitors
Pedone EmiliaMaria
Di Gaetano Sonia
Pirone Luciano
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MRI Tracking of Macrophages Labeled with Glucan Particles Entrapping perfluorocarbons based nanoparticles
Menchise Valeria
Strategy to discover full-length amyloid-beta peptide ligands using high-efficiency microarray technology
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1.453
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Scala S,
Pacelli R
, Iaffaioli RV, Normanno N, Pepe S, Frasci G, Genua G, Tsuruo T, Tagliaferri P, Bianco AR
Reversal of adriamycin resistance by recombinant α-interferon in multidrug-resistant human colon carcinoma LoVo-doxorubicin cells
(
682 views
)
Cancer Res (ISSN: 0008-5472, 1538-7445, 1538-7445electronic)
,
1991 Sep 15;
51(18): 4898-4902.
Impact Factor:
8.426
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Camera L
,
Del Vecchio S
, Petrillo A, Esposito G, Frasci G, Iaffaioli RV, Bianco AR,
Salvatore M
Evaluation of therapeutic response using iodine-131-B72. 3 monoclonal antibody in patients with ovarian carcinoma
(
593 views
)
Eur J Nucl Med (ISSN: 0340-6997, 1619-7070, 1619-7089)
,
1991 Apr;
18(4): 269-273.
Impact Factor:
2.692
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Del Vecchio S
,
Camera L
, Petrillo A, Esposito G, Frasci G, Iaffaioli RV, Bianco AR,
Salvatore M
Clinical studies with B72. 3 in ovarian cancer and probe-guided tumor localization
(
750 views
)
Nucl Med Biol (ISSN: 0883-2897, 0969-8051)
,
1991;
18(1): 85-87.
Impact Factor:
1.042
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Lauro GM,
Fonti R
, Margotta V
Phylogenetic evolution of intermediate filament associated proteins in ependymal cells of several adult poikilotherm vertebrates
(
474 views
)
Journal Fur Hirnforschung (ISSN: 0021-8359)
,
1991;
32(2): 257-261.
Impact Factor:
0
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49
Records (
47
excluding Abstracts).
Total impact factor:
204.898
(
203.53
excluding Abstracts).
Total 5 year impact factor:
214.229
(
212.917
excluding Abstracts).
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Massimiliano Sorbillo
on Sunday 12 July 2020, 13:14:42
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Last view on Saturday 05 October 2024, 0:15:07