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International Journal of Bioprinting                                         AI for sustainable bioprinting


























































            Figure 3. AlphaFold 3 is capable of accurately predicting protein structures, protein–ligand interactions, and multi-component biomolecular complexes
            using its advanced diffusion-based architecture and Pairformer module. (A) The Pairformer module and diffusion-based architecture of AlphaFold 3
            enable precise predictions of biomolecular interactions without reliance on multiple sequence alignments, showcasing its innovative approach to modeling
            complex biological systems. (B) Success rates in predicting diverse biomolecular complexes, including protein–protein, protein–ligand, and protein–nucleic
            acid interactions, highlight its capability to identify key functional interactions relevant for material design. (C) Real-world applications of AlphaFold
            3 in discovering and modeling biomolecular materials: (i) protein–nucleic acid complexes, (ii) protein–ligand systems, and (iii) ribosomal subunits,
            demonstrating its potential to guide the development of bioactive hydrogels and other sustainable bioprinting materials. Reprinted from Abramson et al.
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               Despite AlphaFold’s transformative impact on protein   the available datasets are often small, heterogeneous, and
            modeling, developing comparable AI tools for biomaterial   inaccessible. This hinders model training, validation, and
            design in bioprinting remains limited by fundamental   benchmarking, making it difficult to achieve generalizable
            challenges. One fundamental challenge among these is the   or reproducible outcomes. Additionally, the performance
            absence of large, standardized, and well-annotated open-  of  hydrogels  often  depends  not  only  on  molecular
            source datasets that link bioink composition to rheological   configuration but also on mesoscale properties (e.g.,
            properties, printability, and biological performance.   porosity, swelling, rheology), which are difficult to encode
            Unlike protein sequences with defined formats and   or predict purely from primary composition. Addressing
            abundant data, bioinks lack universal representations, and   these limitations requires community-wide efforts in data

            Volume 11 Issue 4 (2025)                       138                            doi: 10.36922/IJB025170164
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