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International Journal of Bioprinting                                   Printing organoids in peptide matrices


























































            Figure 1. Physicochemical characterizations. (a) Scanning electron microscope (SEM) images of nanofibers generated in different peptide hydrogels. Scale
            bars: 1 µm. (b) Nanofiber topography images of peptide hydrogels captured by atomic force microscopy (AFM). The bottom graphs indicate the height
            distribution for each image. Scale bars: 500 nm. (c) Raman analysis of peptide secondary structures with amide I peak deconvolution. The Raman shift
            of the most represented secondary structure is indicated. (d) Modulus change at different parent peptide concentrations, i.e., 1, 1.5, 2, and 3 mg/mL. (e)
            Modulus of different concentrations of FIB (0.25, 0.5, and 1 mg/mL) mixed with 1 mg/mL of parent peptide. (f) Modulus of different concentrations of
            LAM (0.25, 0.5, 1, and 2 mg/mL) mixed with 1 mg/mL IIFK. The dotted lines in (e) and (f) correspond to the storage modulus (731 Pa) and loss modulus
            (119 Pa) of the parent peptide at 1 mg/mL for comparison. Abbreviations: FIB, fibrinogen-derived peptide containing the RGD motif; LAM, laminin-
            derived peptide containing YIGSR.

            and handedness was obtained from LAM (high) peptides,   observed the  secondary  structure components for  each
            while the least variable supramolecular structures were   peptide as  α-helix,  β-turn,  and unordered structures.
            obtained from FIB (high) peptides. Moreover, LAM (high)   We noticed that all combinations presented a substantial
            peptides result in both left- and right-handed helices   component of  β-turn, whereas the peaks pertaining to
            (Figure 1). Most peptides only portrayed a left-handed   α-helix were non-substantial in all conditions, except in
            configuration which resembles that of collagen helices.    FIB (high) and LAM (low). Unordered structures were
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               Raman spectra also support the observations regarding   detected in all combinations. Moreover, the large full width
            the structure of the peptide hydrogels. In  Figure 1c, we   at half maximum (FWHM) of the β-turn signature for each


            Volume 10 Issue 5 (2024)                       346                                doi: 10.36922/ijb.3033
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