| Reactions of beta-propiolactone with nucleobase analogues, nucleosides, and peptides: implications for the inactivation of viruses. | |
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MedLine Citation:
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PMID: 21868382 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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β-Propiolactone is often applied for inactivation of viruses and preparation of viral vaccines. However, the exact nature of the reactions of β-propiolactone with viral components is largely unknown. The purpose of the current study was to elucidate the chemical modifications occurring on nucleotides and amino acid residues caused by β-propiolactone. Therefore, a set of nucleobase analogues was treated with β-propiolactone, and reaction products were identified and quantified. NMR revealed at least one modification in either deoxyguanosine, deoxyadenosine, or cytidine after treatment with β-propiolactone. However, no reaction products were found from thymidine and uracil. The most reactive sides of the nucleobase analogues and nucleosides were identified by NMR. Furthermore, a series of synthetic peptides was used to determine the conversion of reactive amino acid residues by liquid chromatography-mass spectrometry. β-Propiolactone was shown to react with nine different amino acid residues. The most reactive residues are cysteine, methionine, and histidine and, to a lesser degree, aspartic acid, glutamic acid, tyrosine, lysine, serine, and threonine. Remarkably, cystine residues (disulfide groups) do not react with β-propiolactone. In addition, no reaction was observed for β-propiolactone with asparagine, glutamine, and tryptophan residues. β-Propiolactone modifies proteins to a larger extent than expected from current literature. In conclusion, the study determined the reactivity of β-propiolactone with nucleobase analogues, nucleosides, and amino acid residues and elucidated the chemical structures of the reaction products. The study provides detailed knowledge on the chemistry of β-propiolactone inactivation of viruses. |
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Authors:
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Joost P Uittenbogaard; Bert Zomer; Peter Hoogerhout; Bernard Metz |
Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't Date: 2011-08-25 |
Journal Detail:
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Title: The Journal of biological chemistry Volume: 286 ISSN: 1083-351X ISO Abbreviation: J. Biol. Chem. Publication Date: 2011 Oct |
Date Detail:
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Created Date: 2011-10-17 Completed Date: 2011-12-07 Revised Date: 2013-05-23 |
Medline Journal Info:
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Nlm Unique ID: 2985121R Medline TA: J Biol Chem Country: United States |
Other Details:
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Languages: eng Pagination: 36198-214 Citation Subset: IM |
Affiliation:
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Unit Vaccinology, National Institute for Public Health and the Environment, 3720 BA Bilthoven, The Netherlands. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Disinfectants
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chemistry* Nucleosides / chemistry* Peptides / chemistry* Propiolactone / chemistry* Viral Proteins / chemistry* Virus Inactivation* Viruses / chemistry* |
| Chemical | |
Reg. No./Substance:
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0/Disinfectants; 0/Nucleosides; 0/Peptides; 0/Viral Proteins; 57-57-8/Propiolactone |
| Comments/Corrections | |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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