title: Monomer units for the beta-bend ribbon structure: MeAib peptides.
abstract: A conformational analysis in CDCl3 solution by using i.r. absorption and 1H nuclear magnetic resonance spectroscopy was performed on the fully blocked dipeptides Z-MeAib-Aib-NHMe, Z-MeAib-L-Ala-NHMe, Z-Aib-MeAib-NHMe, and Z-L-Ala-MeAib-NHMe, representing repeating units of the beta-bend ribbon spiral (an approximate 3(10)-helix, with an intramolecular H-bonding donor every two residues), where Z represents benzyloxycarbonyl, MeAib alpha-methylaminoisobutyric acid, and NHMe methylamino. The molecular and crystal structures of the first three compounds were also assessed by X-ray diffraction. While the -MeAib-Aib-, -MeAib-L-Ala-, and -Aib-MeAib- sequences give stable beta-bend structures, the preferred conformation of the -L-Ala-MeAib- sequence is open. These results indicate that the MeAib residue is a good beta-bend promoter, but less efficient than its unmethylated counterpart at position i + 2.
authors.affiliation: Department of Organic Chemistry, University of Padova, Italy.
authors.forename: V
authors.initials: V
authors.lastname: Moretto
authors.forename: G
authors.initials: G
authors.lastname: Valle
authors.forename: M
authors.initials: M
authors.lastname: Crisma
authors.forename: G M
authors.initials: GM
authors.lastname: Bonora
authors.forename: C
authors.initials: C
authors.lastname: Toniolo
mesh_terms: D004151:Dipeptides / Q000737:chemistry*; D006860:Hydrogen Bonding; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D011487:Protein Conformation; D012996:Solutions; D013055:Spectrophotometry, Infrared; D015091:beta-Alanine / Q000031:analogs & derivatives* / Q000737:chemistry
chemical_list: D004151:Dipeptides; D012996:Solutions; D015091:beta-Alanine; C012924:2,2-dimethyl-beta-alanine