Publications by authors named "G Berlier"
Article Synopsis
- The polymerization of unactivated amino acids is significant for industries like medicinal chemistry and prebiotic studies, with silica being a cost-effective promoter for this reaction.
- Despite effective amide/peptide bond synthesis on silica, there is limited understanding of the mechanisms behind this reaction and the factors influencing amino acid (AA) behavior on silica surfaces.
- The review analyzes existing literature on AA adsorption and polymerization mechanisms, discussing how different silica surface properties affect the formation of reaction products and the selectivity in polymerization outcomes.
The application of Cu-CHA catalysts for the selective catalytic reduction of NO by ammonia (NH-SCR) in exhaust systems of diesel vehicles requires the use of fuel with low sulfur content, because the Cu-CHA catalysts are poisoned by higher concentrations of SO. Understanding the mechanism of the interaction between the Cu-CHA catalyst and SO is crucial for elucidating the SO poisoning and development of efficient catalysts for SCR reactions. Earlier we have shown that SO reacts with the [Cu(NH)O] complex that is formed in the pores of Cu-CHA upon activation of O in the NH-SCR cycle.
View Article and Find Full Text PDFThe parameters that determine the formation of linear peptides and cyclic dimers (diketopiperazine, DKP) on silica surfaces of different surface area, silanol and siloxane ring populations, controlled by thermal treatments, are investigated upon glycine deposition from gas and liquid phases. The formed products were characterized by infrared and Raman spectroscopies, X-ray diffraction and thermogravimetric analysis. The results reveal the importance of "nearly-free" silanols to form ester centers as primers for the formation of linear peptides over DKP, on surfaces with medium silanol density (1.
View Article and Find Full Text PDFPeptide formation by amino acids condensation represents a crucial reaction in the quest of the origins of life as well as in synthetic chemistry. However, it is still poorly understood in terms of efficiency and reaction mechanism. In the present work, peptide formation has been investigated through thermal condensation of gas-phase glycine in fluctuating silica environments as a model of prebiotic environments.
View Article and Find Full Text PDFArticle Synopsis
- The study investigates how amino acids, particularly glycine, polymerize into peptides on silica surfaces, which is significant for fields like biotechnology and understanding the origins of life.
- Researchers used infrared spectroscopy at 160 °C to show that glycine reacts with the silica, forming ester species and interacting with silanols, which are key for activating and polymerizing the amino acids.
- The findings suggest that β-turns initiate the growth of polypeptide chains, leading to ordered structures like β-sheets and helices, with water vapor enhancing the formation of stable structures resistant to hydrolysis.