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Updated: Mar 14, 2026

Designing Silk-silk Protein Alloy Materials for Biomedical Applications
Published on: August 13, 2014
Post-translational modifications of silk proteins
Kota Nomura1, Keiji Numata1,2
1Department of Material Chemistry, Graduate School of Engineering, Kyoto University Kyoto 615-8510 Japan keiji.numata@riken.jp.
Abstract:
Post-translational modifications (PTMs) endow silk proteins with chemical diversity that governs their higher-order assembly, hydration, and covalent connectivity. This review highlights the principal PTMs that define silk protein function, including hydroxylation, glycosylation, phosphorylation, and covalent crosslinking. We also describe their contributions to protein structural stability and mechanical properties. Recent advances in proteomics have begun to reveal low-abundance PTMs, whereas synthetic biology and bioorthogonal chemistry enable the programmed installation of modifications to tune physicochemical properties. Understanding and harnessing these chemistries provides a foundation for the predictive design of next-generation protein-based materials at the interface of chemical biology and materials science.
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