1594769-99-9Relevant academic research and scientific papers
Mechanistic insight into the lability of the benzyloxycarbonyl (Z) group in N-protected peptides under mild basic conditions
Tena-Solsona, Marta,Angulo-Pachon, Cesar A.,Escuder, Beatriu,Miravet, Juan F.
, p. 3372 - 3378 (2014/06/09)
An unexpected lability of the benzyloxycarbonyl (Z) protecting group under mild basic conditions at room temperature is explained by a mechanism based on anchimeric assistance. It is found that the vicinal amide group stabilises the tetrahedral intermediate formed after nucleophilic addition of hydroxide to the carbonyl of the Z group. This effect operates in N-protected tripeptides and tetrapeptides but Z-protected dipeptides are stable under the same conditions due to blockage of the vicinal amide NH by intramolecular H-bonding with the terminal carboxylate moiety. Copyright
Tetrapeptidic molecular hydrogels: Self-assembly and Co-aggregation with amyloid fragment Aβ1-40
Tena-Solsona, Marta,Miravet, Juan F.,Escuder, Beatriu
, p. 1023 - 1031 (2014/02/14)
A new family of isomeric tetrapeptides containing aromatic and polar amino acid residues that are able to form molecular hydrogels following a smooth change in pH is described. The hydrogels have been studied by spectroscopic and microscopic techniques showing that the peptide primary sequence has an enormous influence on the self-assembly process. In particular, the formation of extended hydrophobic regions and the appearance of π-stacking interactions have been revealed as the driving forces for aggregation. Moreover, the interaction of these compounds with amyloid peptidic fragment Aβ1-40 has been studied and some of them have been shown to act as templates for the aggregation of this peptide into non-β-sheet fibrillar structures. These compounds could potentially be used for the capture of toxic, soluble amyloid oligomers. Copyright
