Abstract |
A simple, rapid, and highly efficient method for intramolecular disulfide formation in tryptophan-containing peptides using hydrogen peroxide was elaborated. Solid phase synthesis of the peptide fragment corresponding to 601-617 sequence of transmembrane gp41 glycoprotein of HIV-1 was performed by Fmoc-technique. Coupling of Fmoc-Asn- OH by DCC- HOBt method was shown to be accompanied by a side reaction of dehydration of asparagine amide function with the formation of side product (22%) containing 3-cyanoalanine residue. This side reaction was not observed, when Fmoc-Asn- OH was coupled in the form of its p-nitrophenyl ester and with HOBt as a catalyst.
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Authors | M V Sidorova, E V Kudriavtseva, M L Antopol'skiĭ, M E Pal'keeva, M V Ovchinnikov, Zh D Bespalova |
Journal | Bioorganicheskaia khimiia
(Bioorg Khim)
Vol. 22
Issue 4
Pg. 273-9
(Apr 1996)
ISSN: 0132-3423 [Print] Russia (Federation) |
Vernacular Title | Perekis' vodoroda dlia zamykaniia disul'fidnykh sviazeĭ v sinteze peptidov posledovatel'nosti immunodominantnogo epitopa glikoproteina gp41 VICh. |
PMID | 8768265
(Publication Type: English Abstract, Journal Article)
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Chemical References |
- Disulfides
- HIV Envelope Protein gp41
- Immunodominant Epitopes
- Peptide Fragments
- Hydrogen Peroxide
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Topics |
- Amino Acid Sequence
- Disulfides
(chemistry)
- HIV Envelope Protein gp41
(immunology)
- HIV-1
(chemistry)
- Hydrogen Peroxide
(chemistry)
- Immunodominant Epitopes
(chemistry, immunology)
- Molecular Sequence Data
- Peptide Fragments
(chemical synthesis)
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