Self-association of water-soluble peptoids comprising (S)-N-1-(naphthylethyl)glycine residues.
Peptoids (N-substituted glycine oligomers) are widely used peptidomimetics, and an enhanced understanding of their structures is needed to expand their utility, particularly in aqueous applications. We report the synthesis and structural study of four water-soluble peptoids that include strongly helix-promoting (S)-N-1-(naphthylethyl)glycine residues. Peptoid structure changes with both peptoid length and solvent composition. Multiple data support the self-association of the longest peptoid studied here, 1, via hydrophobic interactions in aqueous solutions.
Department of Chemistry & Biochemistry, Santa Clara University , 500 El Camino Real, Santa Clara, California 95053, United States.
Amelia A
AA
Fuller
Brett A
BA
Yurash
Erik N
EN
Schaumann
Frederick J
FJ
Seidl
D002942:Circular Dichroism; D018360:Crystallography, X-Ray; D005998:Glycine / Q000031:analogs & derivatives* / Q000138:chemical synthesis / Q000737:chemistry* / Q000378:metabolism; D057927:Hydrophobic and Hydrophilic Interactions; D034442:N-substituted Glycines / Q000737:chemistry*; D009281:Naphthalenes / Q000138:chemical synthesis / Q000737:chemistry* / Q000378:metabolism; D034444:Peptoids / Q000138:chemical synthesis* / Q000737:chemistry / Q000378:metabolism; D017433:Protein Structure, Secondary; D012997:Solvents / Q000737:chemistry*; D013237:Stereoisomerism; D014867:Water / Q000737:chemistry*
C587471:(S)-N-1-(naphthylethyl)glycine; D034442:N-substituted Glycines; D009281:Naphthalenes; D034444:Peptoids; D012997:Solvents; D014867:Water; D005998:Glycine