Peptide bond formation mediated by 4,5-dimethoxy-2-mercaptobenzylamine after periodate oxidation of the N-terminal serine residue.
[reaction in text] A thiol linker-attached peptide was prepared from a nonprotected peptide via an N(alpha)()-alpha-oxoacyl peptide. Selective oxidation of the N-terminal serine with sodium periodate gave the N(alpha)-glyoxyloyl peptide, reductive amination of which with 4,5-dimethoxy-2-(triphenylmethylthio)benzylamine gave an N(alpha)-4,5-dimethoxy-2-mercaptobenzyl glycyl peptide after removal of the trityl group. The N(alpha)-4,5-dimethoxy-2-mercaptobenzyl peptide can be condensed with a peptide thioester, and the linker is removable. This strategy provides a useful method for the synthesis of peptides using recombinant proteins.
Kawakami
T
T
Institute for Protein Research, Osaka University, 3-2 Yamadaoka, Suita, Osaka 565-0871, Japan.
Akaji
K
K
Aimoto
S
S
D000595:Amino Acid Sequence; D001596:Benzylamines / Q000737:chemistry*; D002851:Chromatography, High Pressure Liquid; D005998:Glycine / Q000737:chemistry; D015394:Molecular Structure; D010084:Oxidation-Reduction; D010455:Peptides / Q000138:chemical synthesis* / Q000737:chemistry*; D020539:Sequence Analysis, Protein; D012694:Serine / Q000737:chemistry; D013329:Structure-Activity Relationship; D013438:Sulfhydryl Compounds / Q000737:chemistry*; D013912:Threonine / Q000737:chemistry
C429243:4,5-dimethoxy-2-mercaptobenzylamine; D001596:Benzylamines; D010455:Peptides; D013438:Sulfhydryl Compounds; D013912:Threonine; D012694:Serine; D005998:Glycine