The influence of structure of isomolecular dipeptides of α-L-alanyl-α-L-alanine and β-alanyl-β-alanine on their behavior in aqueous micellar solution of SDS
| Autor: | M. S. Kurbatova, I. N. Mezhevoi, V. P. Barannikov |
|---|---|
| Rok vydání: | 2020 |
| Předmět: |
Alanine
animal structures Aqueous solution Dipeptide Chemistry 02 engineering and technology 021001 nanoscience & nanotechnology Condensed Matter Physics Branching (polymer chemistry) 01 natural sciences Endothermic process Micelle 010406 physical chemistry 0104 chemical sciences carbohydrates (lipids) Crystallography chemistry.chemical_compound Pulmonary surfactant Zwitterion bacteria Physical and Theoretical Chemistry 0210 nano-technology Instrumentation |
| Zdroj: | Thermochimica Acta. 689:178647 |
| ISSN: | 0040-6031 |
| Popis: | Thermochemical characteristics of α-L-alanyl-α-L-alanine and β-alanyl-β-alanine interactions with SDS micelles at constant surfactant concentration and at various dipeptide contents have been determined. The anion micelles interaction with α-L-alanyl-α-L-alanine is accompanied by endothermic effects, the interaction with β-alanyl-β-alanine being of an exothermic character. The regularities observed may be attributed to different branching of the structure and hydrophobic properties of dipeptides. The tendencies of changing in the average size and ζ-potential of SDS micelles with different additives of dipeptides have also been examined. Additives of zwitterion dipeptides initiate the compensation of a negative charge and the decrease in size of micelles. In range of low concentration of β-alanyl-β-alanine the abrupt increasing of average micelle size is observed, while at high concentration, the micelle size diminishes. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Full Text from ScienceDirect