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The (2‐Phenyl‐2‐trimethylsilyl)ethyl‐(PTMSEL)‐Linker in the Synthesis of Glycopeptide Partial Structures of Complex Cell Surface Glycoproteins
Author(s) -
Wagner Michael,
Dziadek Sebastian,
Kunz Horst
Publication year - 2003
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/chem.200305304
Subject(s) - linker , glycopeptide , chemistry , cleavage (geology) , solid phase synthesis , molecule , glycoprotein , trimethylsilyl , stereochemistry , combinatorial chemistry , muc1 , peptide , mucin , organic chemistry , biochemistry , materials science , fracture (geology) , computer science , composite material , operating system , antibiotics
The (2‐phenyl‐2‐trimethylsilyl)ethyl‐(PTMSEL) linker represents a novel fluoride‐sensitive anchor for the solid‐phase synthesis of protected peptides and glycopeptides. Its cleavage is achieved under almost neutral conditions using tetrabutylammonium fluoride trihydrate in dichloromethane thus allowing the construction of complex molecules sensitive to basic and acidic media commonly required for the cleavage of standard linker systems. The advantages of the PTMSEL linker are demonstrated in the synthesis of glycopeptides from the liver intestine (LI)‐cadherin and the mucin MUC1, bearing carbohydrate moieties such as N‐linked chitobiose or O‐linked sialyl‐T N ‐residues. The synthesis of these types of glycopeptides is difficult because they are prone to secondary structure formation during the synthesis on the solid phase as well as in the completely deprotected form. Using the PTMSEL linker these molecules are accessible by automated synthesis according to the Fmoc strategy without frequently observed side reactions such as aspartimide or diketopiperazine formation.