ArticlePharmaceutical research2016
Thiol-Disulfide Exchange in Human Growth Hormone.
Article in Pharmaceutical research, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 13 citations in OpenAlex.
- Stability of Protein Pharmaceuticals: Recent Advances.Pharmaceutical research · 2024Review
- Mobile Molecules: Reactivity Profiling Guides Faster Movement on a Cysteine Track.Angewandte Chemie (Weinheim an der Bergstrasse, Germany) · 2023Article
- Mobile Molecules: Reactivity Profiling Guides Faster Movement on a Cysteine Track.Angewandte Chemie (International ed. in English) · 2023Article
- Degradation kinetics of α-conotoxin TxID.FEBS open bio · 2019Article
- Identification of Phosphorylated Proteins on a Global Scale.Current protocols in chemical biology · 2018Article
- Recent mass spectrometry-based techniques and considerations for disulfide bond characterization in proteins.Analytical and bioanalytical chemistry · 2018Review
- Peptide modification results in the formation of a dimer with a 60-fold enhanced antimicrobial activity.PloS one · 2017Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
purposeThiol-disulfide exchange was monitored in recombinant human growth hormone (hGH) and in model tryptic peptides derived from hGH to investigate the effects of higher-order structure on the reaction.
methodsDifferent free thiol-containing peptides, varying in length and amino acid sequence, were used to initiate the reaction at pH 7.0 and 37°C in hGH. Protein samples were digested with trypsin and analyzed for native disulfides, scrambled disulfides and free thiols using LC/MS. The loss of native disulfide and disulfide exchange was compared with model peptides derived from hGH.
resultsLoss of native disulfide in cyclic (cT20-T21) and linear peptides (T20-T21pep) derived from the C-terminal hGH disulfide during the first 60 min of reaction was greater than loss of the C-terminal disulfide in hGH itself. Of the thiols tested, glutathione (GSH) was the most reactive, forming the highest percentage of mixed disulfides in intact hGH and in the model peptides. At longer reaction times (>240 min), native disulfides in both hGH and cT20-T21 were regenerated. The fastest rates of regeneration were observed for Cys and the di- or tripeptide containing an Arg residue adjacent to Cys, suggesting that they may be useful in refolding.
conclusionsThiol-disulfide exchange reactions in hGH and related model peptides were influenced by higher order structure, by the size of the thiol reactant and by an Arg residue adjacent to Cys in the thiol reactant. Reduction of disulfide bonds in hGH did not affect higher order structure as measured by CD and HDX-MS.
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Registered trials
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