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Tailored fragments of roseophilin selectively antagonize Mcl-1 in vitro.

ABSTRACT: We have discovered a fragment of the natural product roseophilin, a member of the prodiginine family, that antagonizes Mcl-1 functions in a liposome-based assay for mitochondrial membrane permeabilization. By tailoring this substance such that it can participate in salt bridging with the protein surface, we have prepared the first prodiginine inspired structure that shows direct, saturable binding to a recombinant Bcl-2 family member in vitro.

SUBMITTER: Bracken JD

PROVIDER: S-EPMC4442084 | biostudies-literature | 2015 Jun

REPOSITORIES: biostudies-literature

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Tailored fragments of roseophilin selectively antagonize Mcl-1 <i>in vitro</i>.

Bracken Jack D JD Carlson Andrew D AD Frederich James H JH Nguyen Mai M Shore Gordon C GC Harran Patrick G PG

Tetrahedron letters 20150601 23

We have discovered a fragment of the natural product roseophilin, a member of the prodiginine family, that antagonizes Mcl-1 functions in a liposome-based assay for mitochondrial membrane permeabilization. By tailoring this substance such that it can participate in salt bridging with the protein surface, we have prepared the first prodiginine inspired structure that shows direct, saturable binding to a recombinant Bcl-2 family member <i>in vitro</i>. ...[more]

PMID: 26019371

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