952400-11-2Relevant articles and documents
Studies of β-turn opening with model peptides containing non-coded α-amino isobutyric acid
Dutt, Anita,Dutta, Arpita,Mondal, Raju,Spencer, Elinor C.,Howard, Judith A.K.,Pramanik, Animesh
, p. 10282 - 10289 (2007)
Single crystal X-ray diffraction studies show that among the three terminally protected model tripeptides I-III, Boc-Ile-Aib-Xx-OMe (Xx in peptide I: Val; II: Leu; III: Phe) with a centrally placed non-coded amino acid Aib (Aib: α-amino isobutyric acid), peptide I displays a conformational preference for β-turn, peptide II forms a hydrated β-turn representing the solvent mediated intermediate for the interconversion between β-turn and β-strand and peptide III adopts a completely unfolded β-strand like structure. By varying the steric bulk of the third residue, Xx(3), various conformations related to the structural interconversion between the β-turn and β-strand have been isolated. The peptide conformations in the solution phase have been probed by solvent dependent NMR titration and CD spectroscopy. Morphological studies with scanning electron microscopy (SEM) reveal that among the three peptides only peptide III can form filamentous fibrils in the solid state.
Conformational and self-assembly studies of helix forming hexapeptides containing two α-amino isobutyric acids
Dutt, Anita,Drew, Michael G.B.,Pramanik, Animesh
, p. 549 - 558 (2008/09/16)
Single crystal X-ray diffraction studies reveal that three hexapeptides with general formula Boc-Ile-Aib-Xx-Ile-Aib-Yy-OMe, where Xx and Yy are Leu in peptide I, Leu and Phe in peptide II, and Phe and Leu in peptide III, respectively, adopt equivalent con
