| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 1377240 | Bioorganic & Medicinal Chemistry Letters | 2006 | 4 Pages |
Abstract
We synthesized a series of Δlac-acetogenins in which the two alkyl side chains were systematically modified, and examined their inhibitory effect on bovine heart mitochondrial complex I (NADH-ubiquinone oxidoreductase). The results revealed that the physicochemical properties of the side chains, such as the balance of hydrophobicity and the width (or bulkiness) of the chains, are important structural factors for a potent inhibitory effect of amphiphilic Δlac-acetogenins. This is probably because such properties decide the precise location of the hydrophilic bis-THF ring moiety in the enzyme embedded in the inner mitochondrial membrane.
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Related Topics
Physical Sciences and Engineering
Chemistry
Organic Chemistry
Authors
Naoya Ichimaru, Masato Abe, Masatoshi Murai, Mai Senoh, Takaaki Nishioka, Hideto Miyoshi,