Affiliation:
1. Department of Chemical and Structural Biology, Weizmann Institute of Science, Rehovot 7610001, Israel
Abstract
Significance
Extracellular proteins with mechanical functions often require specialized assembly processes to form covalent oligomers. Progress in tissue bioengineering and repair will benefit from an understanding of how to harness and manipulate these processes. Here, we show that a particular supramolecular assembly mode was pre-encoded in the ancient domain organization common to gel-forming mucins and von Willebrand factor, glycoproteins that are deceptively different due to their divergence for distinct mechanical tasks. This finding highlights symmetry principles and building blocks retooled in nature to construct polymers with wide-ranging properties. These building blocks and knowledge of their self-assembly can be used to design new polymeric structures.
Funder
Israel Science Foundation
Publisher
Proceedings of the National Academy of Sciences
Cited by
10 articles.
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