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Title: Ultrafast biomimetic oxidative folding of cysteine-rich peptides and microproteins in organic solvents
Authors: Kam, Antony
Loo, Shining
Qiu, Yibo
Liu, Chuan-Fa
Tam, James P.
Keywords: Medicine, Health and Life Sciences
Issue Date: 2024
Source: Kam, A., Loo, S., Qiu, Y., Liu, C. & Tam, J. P. (2024). Ultrafast biomimetic oxidative folding of cysteine-rich peptides and microproteins in organic solvents. Angewandte Chemie (International Ed. in English), 63(14), e202317789-.
Project: SYNC 
Journal: Angewandte Chemie (International ed. in English)
Abstract: Disulfides in peptides and proteins are essential for maintaining a properly folded structure. Their oxidative folding is invariably performed in an aqueous-buffered solution. However, this process is often slow and can lead to misfolded products. Here, we report a novel concept and strategy that is bio-inspired to mimic protein disulfide isomerase (PDI) by accelerating disulfide exchange rates many thousand-fold. The proposed strategy termed organic oxidative folding is performed under organic solvents to yield correctly folded cysteine-rich microproteins instantaneously without observable misfolded or dead-end products. Compared to conventional aqueous oxidative folding strategies, enormously large rate accelerations up to 113,200-fold were observed. The feasibility and generality of the organic oxidative folding strategy was successfully demonstrated on 15 cysteine-rich microproteins of different hydrophobicity, lengths (14 to 58 residues), and numbers of disulfides (2 to 5 disulfides), producing the native products in a second and in high yield.
ISSN: 1433-7851
DOI: 10.1002/anie.202317789
Schools: School of Biological Sciences 
Rights: © 2024 Wiley-VCH GmbH. All rights reserved.
Fulltext Permission: none
Fulltext Availability: No Fulltext
Appears in Collections:SBS Journal Articles

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