75666-40-9Relevant academic research and scientific papers
A templating approach for monodisperse self-assembled organic nanostructures
Bull, Steve R.,Palmer, Liam C.,Fry, Nathaniel J.,Greenfield, Megan A.,Messmore, Benjamin W.,Meade, Thomas J.,Stupp, Samuel I.
, p. 2742 - 2743 (2008/09/20)
The precise structural control is known for self-assembly into closed spherical structures (e.g., micelles), but similar control of open structures is much more challenging. Inspired by natural tobacco mosaic virus, we present the use of a rigid-rod template to control the size of a one-dimensional self-assembly. We believe that this strategy is novel for organic self-assembly and should provide a general approach to controlling size and dimension. Copyright
Design of the Synthetic Route for Helical Peptides. Synthesis and Solubility of Model Peptides Having a Helical Structure
Narita, Mitsuaki,Kojima, Yoshihisa,Isokawa, Shizuko
, p. 1976 - 1981 (2007/10/02)
Fragment condensations between amino- and carboxyl-components of hydrophobic decapeptides, which have a β-sheet structure in the solid state and are insoluble in DMF, NMP, and DMSO, were examined in a mixture of CH2Cl2 and TFE (4/1, v/v) using various cou
The Ability of an α-Aminoisobutyric Acid Residue to Promote Helical Folding in Oligopeptides
Narita, Mitsuaki,Ishikawa, Kazunori,Sugasawa, Hiroki,Doi, Masamitsu
, p. 1731 - 1737 (2007/10/02)
In order to investigate the ability of an Aib residue to promote helical folding in oligopeptides, oligo(Leu)s containing an Aib residue were prepared by stepwise elongation and fragment condensation methods.The peptides prepared were the following: Boc-Aib-Leun-OBzl (n=3-6 and 9), Boc-Leun-Aib-OBzl (n=3-6 and 9), Boc-Leu3-Aib-Leu3-OBzl, Boc-Leu4-Aib-Leu4-OBzl, Boc-Leu8-Aib-Leu4-OBzl, Boc-Leu4-Aib-Leu8-OBzl, and Boc-Leu8-Aib-Leu8-OBzl.The IR absorption conformational analyses of Boc-Aib-Leun-OBzl (n=3-6) in dichloromethane have shown the occurrence of incipient helical structures (α- or 310-helixes) formed by one, two, three, and so forth i -> i-4 or i -> i-3 hydrogen-bonding patterns.All the peptides except Boc-Aib-Leu9-OBzl and Boc-Leun-Aib-OBzl (n=6 and 9) have also shown helical structures (α- or 310-helixes), indicating the great ability of an Aib residue to promote helical folding in peptides.This is in remarkable contrast with the fact that homologous oligo(Leu) counterparts have β-sheet structures.The solubility properties of the peptides were in good agreement with those speculated from their conformations.The initiation and stabilization mechanism of helical folding in peptides has been illustrated schematically and attributed to the restriction of the values of the backbone dihedral angles ψ and Ψ of an Aib residue due to steric hindrance, followed by the restriction of the values of ψ and Ψ of other amino acid residues due to hydrogen bonds initiated by the Aib residue.The great ability of an Aib residue to promote helical folding in peptides also suggests that the restriction of the values of the backbone dihedral angles ψ and Ψ (right-handed α-helix: ψ=-57 deg, Ψ=-47 deg) of an amino acid residue in peptide chains is one of important initiation mechanisms of α-helical folding in natural proteins.The implication of the new findings for the study of proteins containing Aib residues is presented on the basis of the stabilizing efficacy of Aib residues on helical regions of proteins.
