Conformational stability of helical peptides containing a thioamide linkage.
[structure: see text] Thioxo peptide analogues of the alpha-helical peptide GCN4-p1 were synthesized and evaluated for helicity and oligomeric state. Sedimentation equilibrium and CD measurements indicate that the thioxo peptides fold into parallel alpha-helical coiled coil structures essentially identical to the native structure. This work marks the first incorporation of a thioamide linkage into the backbone of an alpha-helix and demonstrates that a thioamide linkage is compatible with positions within the helix as well as near the C-terminus.
Miwa
Julia H
JH
Department of Chemistry, Wellesley College, Wellesley, Massachusetts 02481, USA. jmiwa@wellesley.edu
Pallivathucal
Letha
L
Gowda
Shyla
S
Lee
Katherine E
KE
D002942:Circular Dichroism; D004268:DNA-Binding Proteins / Q000737:chemistry; D006860:Hydrogen Bonding; D016350:Leucine Zippers; D010455:Peptides / Q000737:chemistry*; D011494:Protein Kinases / Q000737:chemistry; D017433:Protein Structure, Secondary; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry; D013854:Thioamides / Q000737:chemistry*
D004268:DNA-Binding Proteins; D010455:Peptides; D029701:Saccharomyces cerevisiae Proteins; D013854:Thioamides; D011494:Protein Kinases