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Posttranslationally modified peptides efficiently mimicking neoantigens: A challenge for theragnostics of autoimmune diseases
Author(s) -
Nuti Francesca,
Peroni Elisa,
RealFernández Feliciana,
Bonache M. Angeles,
Le ChevalierIsaad Alexandra,
Chelli Mario,
LubinGermain Nadège,
Uziel Jacques,
Rovero Paolo,
Lolli Francesco,
Papini Anna Maria
Publication year - 2010
Publication title -
peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.21456
Subject(s) - chemistry , glycopeptide , epitope , glycosylation , residue (chemistry) , antibody , stereochemistry , computational biology , combinatorial chemistry , biochemistry , immunology , medicine , biology , antibiotics
We report the design, synthesis, and immunological evaluation of a series of glycopeptide analogues of the previously described antigenic probe CSF114(Glc), with the aim of understanding the importance of N ‐glycosylation on Asn residue in multiple sclerosis antibody recognition. The glucopeptide, characterized by a β‐turn conformation which is fundamental for a correct presentation of the epitope, has been modified by introducing various natural glycoamino acids in position 7. The new glycopeptides were evaluated by measuring the IgG and IgM antibody titer in multiple sclerosis patients' and normal blood donors' sera. Moreover, we achieved the efficient synthetic strategy of new Asn derivative bearing N ‐acetylneuraminic acid (Neu5Ac), linked by an N ‐glycosidic bond, on the side chain of the Asn residue orthogonally protected for Fmoc/tBu SPPS. © 2010 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 94: 791–799, 2010. This article was originally published online as an accepted preprint. The “Published Online” date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at biopolymers@wiley.com