## 4 Materials and Methods
### Molecular Docking  
The molecular docking simulations were conducted on a Dell Precision workstation T7910 equipped with 32 CPU threads. The AutoDock VINA technique, available in the YASARA-Structure software package (version 20.8.23), was utilized for modeling and visualization [41; 42; 43; 44]. Within the YASARA-Structure software, the spatial conformers in 3D of the FEYNF pentapeptide and Drew-Dickerson dodecamer were constructed using the \"BuildMol\" function. Specifically, the FEYNF 3D conformation incorporated the amino acids F-phenylalanyl, E-glutamyl, Y-tyrosineyl, and N-asparaginyl. The dodecamer was formed using the nucleotide sequences of a sense strand 5\({}^{\prime}\)-CGCGAATTCGCG-3\({}^{\prime}\) and a complementary anti-sense strand 3\({}^{\prime}\)-GCGCTTAAGCGC-5\({}^{\prime}\). The 3D structures were subjected to energy minimization (for geometry optimization) at the level of molecular mechanics theory using the YASARA force field. **Supplementary Materials:** The following supporting information can be downloaded at [[https://www.mdpi.com/article/10.3390/gels10020086/s1](https://www.mdpi.com/article/10.3390/gels10020086/s1)]([https://www.mdpi.com/article/10.3390/gels10020086/s1](https://www.mdpi.com/article/10.3390/gels10020086/s1)). Figure S1: The gradient protocol used in HPLC analysis; Figure S2: HPLC chromatogram of the FEYNF-NH\({}_{2}\) peptide following purification through solid-phase extraction, revealing a calculated purity of 99.54%. The chromatogram was generated using an injection volume of 5 \(\mu\)L, and the data were recorded at a detection wavelength of 215 nm. The observed peak patterns and their intensities affirm the successful purification, highlighting the peptide's exceptional purity achieved through the solid-phase extraction process; Figure S3: Visualization of the crystals formed by the HCCA and DHB matrices (a,b) and the co-crystals with the FEYNF samples on the target (c,d). Images obtained by means of the camera equipped with the MALDI-ToF mass spectrometer. Retention times are reported based on HPLC analysis; Figure S4: FTIR spectrum of FEYNF-NH\({}_{2}\) peptide evidencing the amide I-amide II spectral range and the baseline applied for data processing; Table S1: The content of secondary structures (%) of the FEYNF-NH\({}_{2}\) revealed from FTIR spectrum analysis; Figure S5: TEM images of FEYNF-NH\({}_{2}\) before (a) and after 20 h of incubation at physiological pH of 7.4 and a temperature of 37 \({}^{\circ}\)C; EDX spectra for FEYNF peptide sample before (c) and after incubation (d); Figure S6: Microscopic images of FEYNF-NH\({}_{2}\) sample after Congo red staining captured under two polarization angles: 0 degrees (a), and 90 degrees (b); Table S2: Representative clusters of the docking simulation for the FEYNF@FEYNF dimer complex, highlighting the amino acid residues involved in the peptide-peptide interaction, binding energy (\(E_{b}\)) and dissociation constant (\(K_{d}\)) values; Table S3: Intermolecular and intramolecular interactions occurring in the FEYNF@FEYNF dimer complex, with corresponding amino acid residues involved; Figure S7: Graphical representation of (\(\Phi\)j,\(Y\)j) plot (Chain 1: (\(\Phi\)1,\(Y\)1)--red, (\(\Phi\)2,\(Y\)2)--green, (\(\Phi\)3,\(Y\)3)--blue; Chain 2: (\(\Phi\)4,\(Y\)4)--cyan, (\(\Phi\)5,\(Y\)5)--magenta, (\(\Phi\)6,\(Y\)6)--yellow) based on determined torsion angles; Figure S8: Graphical representation of Drew-Dickerson dodecamer sequence (d(CGCGAAATTCCGC)2) with molecular structures of corresponding nitrogenous bases (C-cytosine, G-guanine, A-adenine, T-tymine) and sugar-phosphate backbone (KingDraw V3.0.2.