Peptide segment coupling by prior ligation and proximity-induced intramolecular acyl transfer

Tetrahedron

Volumn 56, Issue 22, 2000, Pages 3449-3491

  Coltart, Don M ^a  

^a UNIVERSITY OF ALBERTA   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE DERIVATIVE; AMIDE; AMINE; CYSTEINE; DIBENZOFURAN; DISULFIDE; GLYCINE DERIVATIVE; IMINE; PEPTIDE; THIAZOLIDINE DERIVATIVE; THIOESTER; THIOL;

AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ARTICLE; CHEMICAL BOND; CHEMICAL REACTION; DNA TEMPLATE; MOLECULAR DYNAMICS; PRIORITY JOURNAL; PROTEIN STRUCTURE; PROTEIN SYNTHESIS; REACTION ANALYSIS;

EID: 0034717002     PISSN: 00404020     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0040-4020(00)00147-2     Document Type: Review

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80. Prepared (see Ref. 22) by reaction of 29.5 (R=OAc) with the cyclohexylamine salt of Cbz-L-Cys(Scm).
81. Kemp D.S., Carey R.I. J. Org. Chem. 54:1989;3640-3646.
82. In other applications (see Ref. 22) of the revised Prior Thiol Capture Strategy (see Scheme 36), non-cysteine side-chains, as well as the α-amino group of the template-linked N-terminal peptide segment (cf. 36.1) were also protected (see Ref. 58).
83. Kemp D.S., Carey R.I. J. Org. Chem. 58:1993;2216-2222.
84. Kemp has explored (see Ref. 56) the use of a novel thiazolidine protecting group as a substitute for Acm. This thiazolidine is potentially advantageous in that it can be hydrolyzed selectively under conditions that are not detrimental to the other thiol protecting groups in the peptide, thus releasing a free thiol group for reaction with ScmCl.
85. The problem of converting the SAcm into the SScm moiety in the presence of the unprotected nucleophilic side-chains of lysine (see Refs. 22,58) and histidine (see Ref. 61) has been studied. Histidine functionalization by ScmCl is suppressed by using formic acid-acetic acid-DMF for conversion of a terminal Cys(Acm) into Cys(Scm).
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98. Kent has developed an efficient procedure for the preparation of this compound. See Ref. 71.
99. Several other peptides besides those discussed in this Review have been made (see Refs. 66,75), but no details are given in the original publications.
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105. The exact form of the C-terminus at this point is not clear from the original publication. The C-terminal peptide is either released from the resin as a thioester, in which case it is presumably used as such, or it is released in the form of a thioacid, in which case it is presumably derivatized as a thioester, and then elaborated.
106. The published results (see Ref. 75) do not indicate whether any attempt was made to separate the two peptides; hence, it is not clear if the C-terminal peptides used in the model ligations 4 and 5 (see Table 9) were pure stereoisomers.
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108. Tam J.P., Rao C., Liu C.-F., Shao J., Int. J. Pep. Protein Res. 45:1995;209-216.
109. The following species has also been used as a solid support for these purposes. See Ref. 23.
110. Liu C.-F., Rao C., Tam J.P. J. Am. Chem. Soc. 118:1996;307-312.
111. For proline surrogates, see: Tam, J. P.; Miao, Z. J. Am. Chem. Soc. 1999, 121, 9013-9022 and references cited therein.
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