Genetic, physiological, and biochemical data indicate that agglomerates of the 42-amino acid form of the amyloid-b (Ab42) peptide are strongly linked to Alzheimer’s disease (AD) etiology and thus represent a particularly attractive target for the development of an effective diseasemodifying approach for AD treatment. A plethora of chemical entities able to modulate Ab42 self-assembly have been developed in recent years, among them, several are in clinical or preclinical development.

Small-molecule inhibitors/modulators of amyloid-β peptide aggregation and toxicity for the treatment of Alzheimer's disease: a patent review (2010 – 2012) / Federica Belluti;Angela Rampa;Silvia Gobbi;Alessandra Bisi. - In: EXPERT OPINION ON THERAPEUTIC PATENTS. - ISSN 1354-3776. - STAMPA. - 23:(2013), pp. 581-596. [10.1517/13543776.2013.772983]

Small-molecule inhibitors/modulators of amyloid-β peptide aggregation and toxicity for the treatment of Alzheimer's disease: a patent review (2010 – 2012)

BELLUTI, FEDERICA;RAMPA, ANGELA;GOBBI, SILVIA;BISI, ALESSANDRA
2013

Abstract

Genetic, physiological, and biochemical data indicate that agglomerates of the 42-amino acid form of the amyloid-b (Ab42) peptide are strongly linked to Alzheimer’s disease (AD) etiology and thus represent a particularly attractive target for the development of an effective diseasemodifying approach for AD treatment. A plethora of chemical entities able to modulate Ab42 self-assembly have been developed in recent years, among them, several are in clinical or preclinical development.
2013
Small-molecule inhibitors/modulators of amyloid-β peptide aggregation and toxicity for the treatment of Alzheimer's disease: a patent review (2010 – 2012) / Federica Belluti;Angela Rampa;Silvia Gobbi;Alessandra Bisi. - In: EXPERT OPINION ON THERAPEUTIC PATENTS. - ISSN 1354-3776. - STAMPA. - 23:(2013), pp. 581-596. [10.1517/13543776.2013.772983]
Federica Belluti;Angela Rampa;Silvia Gobbi;Alessandra Bisi
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11585/190946
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