TY - JOUR
T1 - Folding and self-assembling with β-oligomers based on (1R,2S)-2-aminocyclobutane-1-carboxylic acid
AU - Torres, Elisabeth
AU - Gorrea, Esther
AU - Burusco, Kepa K.
AU - Da Silva, Eric
AU - Nolis, Pau
AU - Rúa, Federico
AU - Boussert, Stéphanie
AU - Díez-Pérez, Ismael
AU - Dannenberg, Samantha
AU - Izquierdo, Sandra
AU - Giralt, Ernest
AU - Jaime, Carlos
AU - Branchadell, Vicen
AU - Ortuño, Rosa M.
PY - 2010/1/1
Y1 - 2010/1/1
N2 - Improved methodologies are provided to synthesize (1R,2S)-2- aminocyclobutane-1-carboxylic acid derivatives and their incorporation into β-peptides of 2-8 residues bearing different N-protecting groups. The conformational analysis of these oligomers has been carried out by using experimental techniques along with theoretical calculations. This study shows that these oligomers adopt preferentially a strand-type conformation in solution induced by the formation of intra-residue six-membered hydrogen-bonded rings, affording cis-fused [4.2.0]octane structural units that confer high rigidity on these β-peptides. Moreover, all of them are prone to self-assemble producing nano-sized fibres, as evidenced by TEM, AFM and SPFM, and, in some instances, they also form gels. These techniques and molecular modelling allowed us to suggest an aggregation model for the assembly structures in which a parallel molecular-arrangement is preferred and the conformation is similar to that observed in solution. According to this model, both hydrogen-bonding and hydrophobic interactions would account for formation of the assemblies. © 2010 The Royal Society of Chemistry.
AB - Improved methodologies are provided to synthesize (1R,2S)-2- aminocyclobutane-1-carboxylic acid derivatives and their incorporation into β-peptides of 2-8 residues bearing different N-protecting groups. The conformational analysis of these oligomers has been carried out by using experimental techniques along with theoretical calculations. This study shows that these oligomers adopt preferentially a strand-type conformation in solution induced by the formation of intra-residue six-membered hydrogen-bonded rings, affording cis-fused [4.2.0]octane structural units that confer high rigidity on these β-peptides. Moreover, all of them are prone to self-assemble producing nano-sized fibres, as evidenced by TEM, AFM and SPFM, and, in some instances, they also form gels. These techniques and molecular modelling allowed us to suggest an aggregation model for the assembly structures in which a parallel molecular-arrangement is preferred and the conformation is similar to that observed in solution. According to this model, both hydrogen-bonding and hydrophobic interactions would account for formation of the assemblies. © 2010 The Royal Society of Chemistry.
U2 - 10.1039/b918755c
DO - 10.1039/b918755c
M3 - Article
SN - 1477-0520
VL - 8
SP - 564
EP - 575
JO - Organic and Biomolecular Chemistry
JF - Organic and Biomolecular Chemistry
IS - 3
ER -