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Self-Assembly of Homo Phenylalanine Oligopeptides: Role of Oligopeptide Chain Length.

Langmuir

January 2025

Biomimetic Materials and Tissue Engineering Laboratory, Department of Chemical Engineering, University of South Carolina, Columbia, South Carolina 29208, United States.

The self-assembly of phenylalanine (F)-based peptides is a critical area of research with potential implications for the development of advanced biomaterials and technologies. Previous studies indicate that homo-oligopeptides with F-X residues (X = 1 to 6) can self-assemble into diverse nano-microstructures, but the role of oligopeptide chain length on this process remains unclear. This review investigates the role of F-X chain length on self-assembly processes and morphologies, considering the effect of incubation conditions and the capping group at the N and/or C terminals.

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Dipeptides were constructed using hydrophobic amino acid residues following AMP prediction. After that Boc-modification was performed on the screened peptides and finally Boc-Phe-Trp-OMe and Boc-Trp-Trp-OMe were synthesized. Even though no inhibition zones were observed in agar well diffusion assays, minimum inhibitory concentration (MIC) analysis revealed anti-bacterial activity against both Gram-positive and Gram-negative bacteria, with MIC ranging from 230 to 400 μg/mL.

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The association of 55 dipeptides extracted from aggregation-prone regions of selected proteins was studied by means of multiplexed replica-exchange molecular dynamics simulations with the coarse-grained UNRES model of polypeptide chains. Each simulation was carried out with 320 dipeptide molecules in a periodic box at 0.24 mol/dm concentration, in the 260-370 K temperature range.

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