## 4 Conclusions
The narrowing of the amide I band and the shift of the peak center to lower wavenumber after methanol treatment indicates a greater contribution arising from \(\beta\)-sheets. ; Figure S3. Antimicrobial activity of non-functionalized SELP (SELP-59-A without AMPs) assessed by direct contact with the surface of the films against E. coli and S. aureus. Cell suspensions inoculated in empty wells were used as reference for 100% survival. No statistically significant differences were observed between SELP films and the control, indicating the absence of antimicrobial activity; Table S1: List of genetic constructions used in this work. Molecular weight was calculated with Expasy Compute pI/Mw tool ([[https://web.expasy.org/compute_pi/](https://web.expasy.org/compute_pi/)]([https://web.expasy.org/compute_pi/](https://web.expasy.org/compute_pi/)); accessed on 30 October 2020); Table S2: Amino acid sequence and size of antimicrobial peptides. Molecular weight was calculated with Expasy Compute pI/Mw tool ([[https://web.expasy.org/compute_pi/](https://web.expasy.org/compute_pi/)]([https://web.expasy.org/compute_pi/](https://web.expasy.org/compute_pi/)); accessed on 30 October 2020); Table S3: Vibrational band assignments used for conformational structure quantification ([PERSON] et al., 2006; [PERSON] et al., 2015; [PERSON] et al., 2017); Table S4: Number of CFUs obtained in the antimicrobial assays of AMP-SELP and AMP-A200 films against Escherichia coli. Experiments were performed in triplicate in independent days (\(n=1\), \(n=2\) and \(n=3\)) with three replicas each. Each value corresponds to the number of CFUs obtained in a plate after a 1:20 dilution in sterile saline solution. Each set of three values correspond to replicates. Letters in superscript correspond to the respective control in each independent day (\(n\)). Values between brackets were excluded from statistical analysis due to high deviating values or due to contamination; Table S5: Number of CFUs obtained in the antimicrobial assays of AMP-SELP and AMP-A200 films against Staphylococcus aureus. Experiments were performed in triplicate in independent days (\(n=1\), \(n=2\) and \(n=3\)) with three replicas each. Each value corresponds to the number of CFUs obtained in a plate after a 1:20 dilution in sterile saline solution. Each set of three values corresponds to replicates. Letters in superscript correspond to the respective control in each independent day (\(n\)). Values between brackets were excluded from statistical analysis due to high deviating values or due to contamination; Table S6: Amino acid sequences of constructions. Genetic constructions were obtained by standard genetic engineering techniques using DNA sequences optimized for Escherichia coli codon usage. Genetic sequences coding for AMPs were cloned at the N-terminus of A200 and SELP polymers and were chemically synthesized with flanking _NdeI_ and _KpnI_ restriction sites (A200-based constructions) or with flanking _NdeI_ restriction sites (SELP-based constructions). The full amino acid sequences are presented below. The sequences coding for the AMPs are in red color and emphasized in bold. Conceptualization, A.M.P., M.C. and R.M. ; methodology, A.M.P., D.G., A.d.C. and R.M. ; software analysis, A.M.P. and R.M. ; validation, A.M.P., D.G., A.d.C., M.C. and R.M. ; formal analysis, A.M.P. and R.M. ; investigation, A.M.P., D.G. and A.d.C. ; resources, S.C.D., M.C. and R.M. ; data curation, A.M.P. and D.G. ; writing--original draft preparation, A.M.P. ; writing--review and editing, D.G., A.d.C., S.C.D., M.C. and R.M. ; supervision, M.C. and R.M. ; funding acquisition, M.C. and R.M. All authors have read and agreed to the published version of the manuscript. This work was supported by the \"Contrao-Programa\" UIDB/04050/2020, project FunBioPlas (ERA-IB-2-6/0004/2014) and project FUN2 CYT (POCI-01-0145-FEDER-030568) funded by Portugal national funds through the Fundacao para a Ciencia e a Tecnologia (FCT LP). A.M.P.