Regards,
Igor
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1. IVANOV BB, ROBEY FA: Effective use of free thiols as scavengers for
HF cocktails to deprotect bromo- and chloroacetylated synthetic
peptides. Pept Res 1996, 9:305-307.
Abstract: A variety of thiol-containing compounds, in combination with
p-cresol, were tested as scavengers in hydrogen fluoride (HF) cocktails
that are used to deprotect haloacetylated peptidyl resins. Our results
indicate that brome and chloroacetyl moieties on a synthetic peptide
remain intact following HF treatment when the HF cocktail contains
m-cresol along with either thiophenol, m-thiocresol or
1,2-ethanedithiol. The free thiols prevent the formation of a number of
impurities in the preparation of bromo- and chloroacetylated peptides
that contain amino acids that could be oxidized in a nonreducing HF
environment. Ethvimethylsulfide, however, could not be used with
bromoacetylated peptides, but it could be used with chloroacetylated
peptides
2. KOLODNY N, ROBEY FA: Conjugation of synthetic peptides to proteins:
quantitation from S- carboxymethylcysteine released upon acid
hydrolysis. Anal Biochem 1990, 187:136-140.
Abstract: A method described here for conjugating synthetic peptides to
carrier proteins provides a convenient method for determining
peptide-to- carrier protein ratios. N-Bromoacetyl-containing peptides
are reacted in situ with carrier proteins in which the disulfide bonds
were reduced with tri-n-butylphosphine. At pH 7-8 and ambient
temperature, the newly formed sulfhydryl groups of the carrier protein
react exclusively with the bromoacetyl mokiety of the peptide to form
conjugates having stable thio ether linkages. Acid hydrolyses of these
conjugates release S- carboxymethylcysteine in amounts proportional to
the amounts of peptides conjugated and thus allow determination of
peptide-to-protein ratios
3. ROBEY FA, FIELDS RL: Automated synthesis of N-bromoacetyl-modified
peptides for the preparation of synthetic peptide polymers,
peptide-protein conjugates, and cyclic peptides. Anal Biochem 1989,
177:373-377.
Abstract: A method to incorporate N-bromoacetyl moieties at the amino
termini of synthetic peptides using a standard program with an automated
peptide synthesizer has been developed. The N-bromoacetyl-derivatized
peptides react well with sulfhydryl-containing proteins and with
peptides containing cysteine residues. Autopolymerization or cyclization
occurs by reaction of the free sulfhydryl of cysteine in a peptide with
the bromoacetyl group and reactions can generally be controlled by
controlling the concentrations of starting peptide in neutral pH
buffers. Analytical methods for evaluating the polymers or cyclized
peptides include gel filtration chromatography, reverse phase HPLC,
sodium dodecyl sulfate-polyacrylamide gel electrophoresis, and amino
acid analysis where the degree of reaction can be evaluated by
quantifying the amount of S-carboxymethylcysteine formed after HCl
hydrolysis. N-Bromoacetyl-derivatized peptides may be useful as reagents
for potential peptide immunogens, vaccines, and therapeutics and as
intermediates in the production of solid supports with peptide surfaces
4. ROBEY FA: Bromoacetylated synthetic peptides. Starting materials for
cyclic peptides, peptomers, and peptide conjugates. Methods Mol Biol
1994, 35:73-90.
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Original message
>Hi, everyone
>I would like to synthesize several N-term bromoacetamido peptides. I
wonder if I can use the standard solid phase way for that purpose, the
main question beeing the compatibility of that function with classical
cleavage-deprotection cocktail mixtures(obviously without EDT).
>Thanks for any advice.
>Jean LUCCHETTI, Ph.D.
------------------------------------------------
Igor L. Rodionov
E-mail: <rodionov@fibkh.serpukhov.su>
Laboratory of Peptide Chemistry
Branch of Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry
Pushchino, Moscow Region
142292, Russian Federation