Use of Mpc-amino acids in solid phase peptide synthesis leads to improved coupling efficiencies.
The Mpc-group has a somewhat better stability than the Fmoc-group, resists catalytic hydrogenolysis, is highly stable in acidic media and its elimination product does not polymerize spontaneously. In a direct comparison of coupling efficiencies obtained in solid phase peptide syntheses using Mpc- or Fmoc-amino acids it is shown that the use of Mpc-amino acids leads to better coupling efficiencies and, consequently, a more homogeneous peptide. An improved synthesis of Mpc-ONSu and of Mpc-amino acid derivatives is presented.
Schielen
W J
WJ
Laboratory of Organic Chemistry, University of Nijmegen, Leiden, The Netherlands.
Adams
H P
HP
Nieuwenhuizen
W
W
Tesser
G I
GI
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000737:chemistry; D000603:Amino Acids, Sulfur / Q000737:chemistry*; D055598:Chemical Phenomena; D002621:Chemistry; D005340:Fibrinogen / Q000138:chemical synthesis; D005449:Fluorenes; D008969:Molecular Sequence Data; D015394:Molecular Structure; D010446:Peptide Fragments / Q000138:chemical synthesis; D010455:Peptides / Q000138:chemical synthesis*; D013450:Sulfones / Q000737:chemistry*
D000596:Amino Acids; D000603:Amino Acids, Sulfur; D005449:Fluorenes; C016456:N(alpha)-fluorenylmethyloxycarbonylamino acids; D010446:Peptide Fragments; D010455:Peptides; D013450:Sulfones; D005340:Fibrinogen