Effect of copper salts on peptide bond formation using peptide thioesters.
[reaction: see text] In the present paper, systematic studies revealed that Cu(I) salts in general and Cu(II) salts under certain circumstances promote effective reaction between peptide thiol esters and the N-terminal amino function of a second peptide segment to give the native amide bond for both solution- and solid-phase syntheses. Chiral integrity was retained. Reaction conditions were optimized and applied to the synthesis of a small protein, the identity of which was confirmed by NMR analysis.
Ingenito
Raffaele
R
Jerini Peptide Technologies a Division of Jerini AG, Invalidenstr. 130, 10115 Berlin, Germany. raffaele_ingenito@merck.com
Wenschuh
Holger
H
D000215:Acylation; D003300:Copper / Q000737:chemistry*; D004952:Esters / Q000737:chemistry*; D005998:Glycine / Q000737:chemistry; D007930:Leucine / Q000737:chemistry; D010455:Peptides / Q000138:chemical synthesis* / Q000737:chemistry*; D010649:Phenylalanine / Q000737:chemistry; D013438:Sulfhydryl Compounds / Q000737:chemistry*; D013997:Time Factors
D004952:Esters; D010455:Peptides; D013438:Sulfhydryl Compounds; D010649:Phenylalanine; D003300:Copper; D007930:Leucine; D005998:Glycine