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Article

Small molecules block the polymerization of Z alpha1-antitrypsin and increase the clearance of intracellular aggregates.

Journal of medicinal chemistry - 1 Nov 2007

Mallya Meera, Phillips Russell L, Saldanha S Adrian, Gooptu Bibek, Brown Sarah C Leigh, Termine Daniel J, Shirvani Arash M, Wu Ying, Sifers Richard N, Abagyan Ruben, Lomas David A

Abstract excerpt

The Z mutant of alpha1-antitrypsin (Glu342Lys) causes a domain swap and the formation of intrahepatic polymers that aggregate as inclusions and predispose the homozygote to cirrhosis. We have identified an allosteric cavity that is distinct from the interface involved in polymerization for rational structure-based drug design to block polymer formation. Virtual ligand screening was performed on 1.2 million small...

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Identifiers

PMID: 17918823
DOI: 10.1021/jm070687z
PMCID: PMC2631427

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Small molecules block the polymerization of Z alpha1-antitrypsin and increase the clearance of intracellular aggregates.PMID 17918823Read ↗

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