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- W2068888950 abstract "Abstract PA1b (Pea Albumin 1, subunit b) is a hydrophobic, 37‐amino acid miniprotein isolated from pea seeds ( Pivum sativum ), crosslinked by three interlocked disulfide bridges, signature of the ICK (inhibitory cystine‐knot) family. It acts as an entomotoxic factor against major insect pests in stored crops and vegetables, making it a promising bioinsecticide. Here we report an efficient and simple protocol for the production of large quantities of highly pure, biologically active synthetic PA1b. The features of PA1b oxidative refolding revealed the off‐pathway products and competitive aggregation processes. The efficiency of the oxidative folding can be significantly improved by using hydrophobic alcoholic cosolvents and decreasing the temperature. The homogeneity of the synthetic oxidized PA1b was established by reversed‐phase HPLC. The correct pairing of the three disulfide bridges, as well as the three‐dimensional structure of synthetic PA1b was assessed by NMR. Synthetic PA1b binds to microsomal proteins from Sitophilus oryzae with a Kd of 8 n M , a figure quite similar to that determined for PA1b extracted from its natural source. Moreover, the synthetic miniprotein was as potent as the extracted one towards the sensitive strains of weevils. Our findings will open the way to the production of PA1b analogues by chemical means to an in‐depth understanding of the PA1b mechanism of action. © 2009 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 92: 436–444, 2009. This article was originally published online as an accepted preprint. The “Published Online” date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at biopolymers@wiley.com" @default.
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- W2068888950 date "2009-01-01" @default.
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- W2068888950 title "A folded and functional synthetic PA1b: An interlocked entomotoxic miniprotein" @default.
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- W2068888950 doi "https://doi.org/10.1002/bip.21217" @default.
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