4.7 Article

Effect of Newly Synthesized Structures of Peptides on the Stability of the Monolayers Formed

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MDPI
DOI: 10.3390/ijms24054318

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Langmuir monolayer; compression isotherm; peptides; TG; DTG; DSC; molecular dynamics simulations

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The aim of the study was to evaluate the effect of different peptide structures on their physiochemical properties. The peptides showed high thermal stability and formed expanded liquid monolayers. Non-polar side chains played an important role in the properties of the peptides. The structure of the peptide affected its physicochemical and layer-forming properties.
The aim of the study was to evaluate the effect of the peptide structure (WKWK)(2)-KWKWK-NH2, P4 (C12)(2)-KKKK-NH2, P5 (KWK)(2)-KWWW-NH2, P6 (KK)(2)-KWWW-NH2 on their physicochemical properties. The thermogravimetric method (TG/DTG) was used, which made it possible to observe the course of chemical reactions and phase transformations occurring during the heating of solid samples. Based on the DSC curves, the enthalpy of the processes occurring in the peptides was determined. The influence of the chemical structure of this group of compounds on their film-forming properties was determined using the Langmuir-Wilhelmy trough method and was followed by molecular dynamics simulation. Evaluated peptides showed high thermal stability and the first significant mass loss occurred only at about 230 degrees C and 350 degrees C. The analysis of the compressibility coefficient of individual peptides indicates that all formed peptide monolayers were in the expanded liquid phase. Their maximum compressibility factor was less than 50.0 mN/m. Its highest value of 42.7 mN/m was achieved in a monolayer made of P4. The results obtained in molecular dynamic simulation indicate that non-polar side chains played an important role in the properties of the P4 monolayer, and the same applies to P5, except that a spherical effect was observed here. A slightly different behavior was observed for the P6 and P2 peptide systems, where the type of amino acids present had an influence. The obtained results indicate that the structure of the peptide affected its physicochemical and layer-forming properties.

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