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Synthesis of cyclic herpes simplex virus peptides containing 281–284 epitope of glycoprotein D‐1 in endo ‐ or exo‐ position
Author(s) -
Mezö Gábor,
Majer Zsuzsa,
Valero MariLuz,
Andreu David,
Hudecz Ferenc
Publication year - 1999
Publication title -
journal of peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 66
eISSN - 1099-1387
pISSN - 1075-2617
DOI - 10.1002/(sici)1099-1387(199906)5:6<272::aid-psc192>3.0.co;2-9
Subject(s) - epitope , chemistry , side chain , stereochemistry , herpes simplex virus , peptide , cyclic peptide , thioanisole , cleavage (geology) , sequence (biology) , peptide sequence , orthogonality , glycoprotein , peptide synthesis , combinatorial chemistry , biochemistry , virus , virology , organic chemistry , antibody , biology , mathematics , catalysis , paleontology , fracture (geology) , gene , immunology , polymer , geometry
We have prepared two types of cyclopeptides containing the 281 DPVG 284 sequence from the 276–284 region of glycoprotein gD‐1 of the Herpes simplex virus (HSV). The syntheses were performed by solid phase methodology using MBHA or BHA resin and orthogonal protection schemes. Head‐to‐side‐chain cyclization included the N‐terminal part of the epitope, while side‐chain‐to‐side‐chain lactam bridge formation resulted in a peptide containing a C‐terminal cycle. Peptides elongated by Cys at the N‐terminal of the sequence were also prepared. Boc chemistry using Fmoc and OFm orthogonal protection was applied for on‐resin cyclization. Based on the orthogonality of Bzl and cHex esters under a 1 m TMSOTf‐thioanisole/TFA cleavage condition, a new approach for the cyclization on BHA‐resin has also been developed. Preliminary studies on solution conformation of the cyclic peptides by CD spectroscopy indicated the importance of the location and the size of the cycle within the epitope sequence. Copyright © 1999 European Peptide Society and John Wiley & Sons, Ltd.