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Volume 166, 2013
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Self-assembling amphipathic alpha-helical peptides induce the formation of active protein aggregates in vivo

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Abstract

We recently found that several self-assembling alpha, beta, or surfactant-like peptides, when terminally attached to proteins, can promote the in vivo assembly of active protein aggregates (or active inclusion bodies, AIBs) in Escherichia coli. In this work, we systematically examined the AIBs induced by an amphipathic α-helical peptide 18Awt (EWLKAFYEKVLEKLKELF) and its variants with altered ion pairs. Transmission electron microscopic and Fourier transform infrared spectroscopic analyses suggested that the AIBs appeared to adopt an amorphous mesh-like structure, and were likely induced by helical structures formed by the assembly of the 18A peptides. Confocal fluorescent micrographic analysis revealed that the AIBs resided around the periphery of the cell membrane or in the cytoplasm, depending on the distribution of ion pairs on the 18A peptides, which suggested that the association between the aggregates and the cell membrane was mediated by the lipid–18A interaction. Two of these 18A peptide variants were further used in constructing cleavable self-aggregating tags (cSAT) in conjunction with an intein molecule for protein purification, and verified using two model proteins. This extends the cSAT approach for laboratory and potentially industrial uses. Our study might also provide new insights into aggregation-related diseases.

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Publication details

The article was received on 29 Apr 2013, accepted on 02 Jul 2013 and first published on 23 Sep 2013


Article type: Paper
DOI: 10.1039/C3FD00068K
Citation: Faraday Discuss., 2013,166, 243-256
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    Self-assembling amphipathic alpha-helical peptides induce the formation of active protein aggregates in vivo

    Z. Lin, B. Zhou, W. Wu, L. Xing and Q. Zhao, Faraday Discuss., 2013, 166, 243
    DOI: 10.1039/C3FD00068K

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