Boc-D-glutamic acid γ-benzyl ester Merrifield resin
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Boc-D-glutamic acid γ-benzyl ester Merrifield resin

* Please kindly note that our products are not to be used for therapeutic purposes and cannot be sold to patients.

Category
Other Resins
Catalog number
BAT-002304
Synonyms
Boc-D-Glu(OBzl)-Merrifield resin
DVB Crosslinking
1% DVB
Mesh Size
100-200 mesh
Substitution
0.8-1.2 meq/g
Storage
Store at 2-8 °C
1. Solid phase synthesis of the protected 27--42 hexadecapeptide of the heavy chain from myeloma immunoglobulin M603. Elimination of side reactions associated with glycyl-2-oxypropionyl-resin
F S Tjoeng, J P Tam, R B Merrifield Int J Pept Protein Res. 1979;14(3):262-74. doi: 10.1111/j.1399-3011.1979.tb01932.x.
A fully protected 27--42 hexadecapeptide of the variable region of myeloma immunoglobulin M603 was synthesized on a 2-bromopropionyl-resin by the solid phase method. Side reactions due to cyclization of glycyl-2-oxypropionyl-resin were studied under different reaction conditions. The loss of peptide chains at the dipeptide and tripeptide stages due to diketopeperazine formation was also examined. These side reactions were circumvented by using a combination of fragment and stepwise coupling methods. The synthesized protected peptide was removed from the resin in 85% yield by photolysis, and purified by crystallization and by chromatography on a Sephadex LH-60 column.
2. Synthesis of the protected tridecapeptide (56-68) of the VH domain of mouse myeloma immunoglobulin M603 and its reattachment to resin supports
C Voss, R Dimarchi, D B Whitney, F S Tjoeng, R B Merrifield, J P Tam Int J Pept Protein Res. 1983 Aug;22(2):204-13. doi: 10.1111/j.1399-3011.1983.tb02087.x.
A protected tridecapeptide, representing a new peptide corresponding to residues 56-68 of the VH domain in the mouse M603 myeloma protein, has been prepared by solid phase peptide synthesis. The protected tridecapeptide was prepared using the photolabile 4-bromomethyl-(3-nitro)-benzamidomethyl-resin and the multidetachable 2-[4-bromomethyl)phenylacetoxy]propionyl-resin as solid supports. The synthetic protocol and protecting groups were the same for both syntheses. The protected tridecapeptide was removed photolytically from both supports and the sequence integrity was determined by preview analysis using the solid phase Edman degradation procedure. The protected tridecapeptide-OMPA was purified to homogeneity by DMF/H2O precipitation and LH-60 chromatography. The purity of the protected peptide was further demonstrated by high pressure liquid chromatography on the free peptide after HF deprotection. The protected tridecapeptide was reattached to 4-bromomethyl-(3-nitro)-benzamidomethyl-resin to give the photolabile Boc-(protected)peptidyl-4-oxymethyl-(3-nitro)benzamidomethyl-resin in 25% yield. The protected tridecapeptide-oxymethylphenylacetic acid derivative was reattached to aminomethyl-resin to give Boc-(protected)peptidyl-2-[4-oxymethyl)phenyl]acetamidomethyl-resin in 45% yield and to 2-bromopropionyl-resin generating the multidetachable Boc-(protected)peptidyl-2-[(4-oxymethyl)phenylacetoxy] propionyl-resin in 80% yield. The reactivity of these reattached peptides was demonstrated by the quantitative coupling of Boc-leucine to the protected peptide-resin. The advantages and disadvantages of the different resins with respect to solid phase fragment synthesis are discussed.
3. Quantitative solid-phase Edman degradation for evaluation of extended solid-phase peptide synthesis
G R Matsueda, E Haber, M N Margolies Biochemistry. 1981 Apr 28;20(9):2571-80. doi: 10.1021/bi00512a032.
Quantitative solid-phase Edman degradation was used for the amino acid sequence analysis of synthetic peptidyl-resins prepared by the Merrifield solid-phase procedure. A model peptide, Ala-[3H]Pro-Ala-Gly-Phe-Ala-Gly-, was synthesized on a solid support and was sequenced to measure the efficiency of the solid-phase sequencing protocol used. An average of 92% of the first four residues was removed from the peptidyl-resin as indicated by subtractive amino acid analysis. Quantitation of the radioactive proline residue at cycle 2 revealed that it was efficiently recovered both from the acid conversion procedure (99%) and also following high-pressure liquid chromatography of the phenylthiohydantoin (Pth) amino acid (88%). In order to facilitate identification and quantification of the side chain protected Pth amino acids, we prepared these derivatives and characterized them by high-pressure liquid chromatography. Thereafter, by the use of solid-phase Edman degradation as an analytical procedure, the synthesis of residues 2-118 of the heavy-chain variable region (VH) of a homogeneous rabbit antibody was undertaken. At 10-15-residue intervals during the solid-phase synthesis, samples of peptidyl-resin were removed from the synthesis vessel and sequenced. When gross synthetic errors caused by deletion of amino acids residues were detected, the solid-phase synthesis was terminated and restarted by using modified protocols. A 117-residue peptidyl-resin was prepared finally which possessed the desired amino acid sequence as indicated by a series of solid-phase Edman degradation experiments. In the final degradation experiment on the 117-residue peptidyl-resin, a 92% efficiency for the automatic Edman reaction was measured ([3H]Leu, penultimate amino-terminal residue). We have found two advantages for the concurrent use of solid-phase Edman degradation during an extended solid-phase synthesis: (1) on the basis of the level of error due to incomplete incorporation of amino acids, the solid-phase assembly could be terminated in favor of restarting the synthesis, hence avoiding further work on a defective product and (2) direct verification of incorporation of amino acids, which during acid hydrolysis are destroyed (Cys, Trp) or are deamidated (Asn, Gln), is possible by high-pressure liquid chromatography of the corresponding Pth derivatives.
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