English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Plus annual

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Tools annual

Global: Zendy Free Plan

Global: Zendy Tools monthly

Global: Zendy Plus monthly

Background  Inactive protein inclusion bodies occur commonly in  Escherichia coli  ( E. coli ) cells expressing heterologous proteins. Previously several independent groups have found that active protein aggregates or pseudo inclusion bodies can be induced by a fusion partner such as a cellulose binding domain from  Clostridium cellulovorans  (CBDclos) when expressed in  E. coli . More recently we further showed that a short amphipathic helical octadecapeptide 18A (EWLKAFYEKVLEKLKELF) and a short beta structure peptide ELK16 (LELELKLKLELELKLK) have a similar property.    Results  In this work, we explored a third type of peptides, surfactant-like peptides, for performing such a "pulling-down" function. One or more of three such peptides (L 6 KD, L 6 K 2 , DKL 6 ) were fused to the carboxyl termini of model proteins including  Aspergillus fumigatus  amadoriase II (AMA, all three peptides were used),  Bacillus subtilis  lipase A (LipA, only L 6 KD was used, hereinafter the same),  Bacillus pumilus  xylosidase (XynB), and green fluorescent protein (GFP), and expressed in  E. coli . All fusions were found to predominantly accumulate in the insoluble fractions, with specific activities ranging from 25% to 92% of the native counterparts. Transmission electron microscopic (TEM) and confocal fluorescence microscopic analyses confirmed the formation of protein aggregates in the cell. Furthermore, binding assays with amyloid-specific dyes (thioflavin T and Cong red) to the AMA-L 6 KD aggregate and the TEM analysis of the aggregate following digestion with protease K suggested that the AMA-L 6 KD aggregate may contain structures reminiscent of amyloids, including a fibril-like structure core.    Conclusions  This study shows that the surfactant-like peptides L 6 KD and it derivatives can act as a pull-down handler for converting soluble proteins into active aggregates, much like 18A and ELK16. These peptide-mediated protein aggregations might have important implications for protein aggregation  in vivo , and can be explored for production of functional biopolymers with detergent or other interfacial activities.

Small surfactant-like peptides can drive soluble proteins into active aggregates