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Progress in the preparation of peptide aldehydes via polymer supported IBX oxidation and scavenging by threonyl resin
Author(s) -
Sorg Gerhard,
Thern Bernd,
Mader Oliver,
Rademann Jörg,
Jung Günther
Publication year - 2005
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/psc.606
Subject(s) - peptide , chemistry , combinatorial chemistry , residue (chemistry) , aldehyde , peptide synthesis , proteolysis , solid phase synthesis , proteasome , organic chemistry , enzyme , biochemistry , catalysis
Peptide aldehydes are of interest due to their inhibitory properties toward numerous classes of proteolytic enzymes such as caspases or the proteasome. A novel access to peptide aldehydes is described using a combination of solid phase peptide synthesis with polymer‐assisted solution phase synthesis based on the oxidation of peptide alcohols with a mild and selective polymer‐bound IBX derivative. The oxidation is followed by selective purification via scavenging the peptide aldehyde in a capture‐release procedure using threonine attached to an aminomethyl resin. Peptide aldehydes are obtained in excellent purity and satisfying yield. The optical integrity of the C ‐terminal residue is conserved in a high degree. The procedures are compatible with the use of common side‐chain protecting groups. The potential for using the method in parallel approaches is very advantageous. A small collection of new and known peptide aldehydes has been tested for inhibitory activity against caspases 1 and 3. Copyright © 2004 European Peptide Society and John Wiley & Sons, Ltd.