Fig. 1

Physicochemical properties of the non-cross-linked ADM. A Gross view of freeze-dried ADM and ADM soaked in PBS; scale bar: 5 mm. B Scanning electron micrographs of ADM. White scale bar:100 μm; red scale bar: 2 μm. C Histogram of the porosity of the basement membrane and papillary dermis of the ADM (n = 3). D–F HE, Masson, and propidium iodide staining of non-cross-linked ADM; scale bar: 100 μm. G Histogram of the pore diameter of the basement membrane and papillary dermis of the ADM. H Components of the ADM patch were identified by FTIR. Collagen structures can be analysed by amide A (3287 cm⁻¹), which reflects the stable triple helix structure formed by hydrogen bonds and amide I (1630 cm⁻¹), amide II (1540 cm⁻¹), and amide III (1240 cm⁻¹), which reflect the secondary structure of collagen (triple helix structure). I Tensile strength control of ADM in PBS and K-SFM (n = 3). *P < 0.05, **P < 0.01, ***P < 0.001