Polymers with controlled assembly and rigidity made with click-functional peptide bundles

Journal Article · Wed Oct 30 00:00:00 EDT 2019 · Nature (London)

DOI:https://doi.org/10.1038/s41586-019-1683-4· OSTI ID:1633855

Wu, Dongdong ^[1]; Sinha, Nairiti ^[2]; Lee, Jeeyoung ^[2]; Sutherland, Bryan P. ^[2]; Halaszynski, Nicole I. ^[2]; Tian, Yu ^[2]; Caplan, Jeffrey ^[2]; Zhang, Huixi Violet ^[3]; Saven, Jeffery G. ^[3]; Kloxin, Christopher J. ^[2]; Pochan, Darrin J. ^[2]

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1. Univ. of Delaware, Newark, DE (United States); University of Delaware
2. Univ. of Delaware, Newark, DE (United States)
3. Univ. of Pennsylvania, Philadelphia, PA (United States)

The engineering of biological molecules is a key concept in the design of highly functional, sophisticated soft materials. Biomolecules exhibit a wide range of functions and structures, including chemical recognition (of enzyme substrates or adhesive ligands, for example), exquisite nanostructures (composed of peptides, proteins or nucleic acids), and unusual mechanical properties (such as silk-like strength, stiffness, viscoelasticity and resiliency). Here we combine the computational design of physical (noncovalent) interactions with pathway-dependent, hierarchical ‘click’ covalent assembly to produce hybrid synthetic peptide-based polymers. The nanometre-scale monomeric units of these polymers are homotetrameric, α-helical bundles of low-molecular-weight peptides. These bundled monomers, or ‘bundlemers’, can be designed to provide complete control of the stability, size and spatial display of chemical functionalities. The protein-like structure of the bundle allows precise positioning of covalent linkages between the ends of distinct bundlemers, resulting in polymers with interesting and controllable physical characteristics, such as rigid rods, semiflexible or kinked chains, and thermally responsive hydrogel networks. Chain stiffness can be controlled by varying only the linkage. Moreover, by controlling the amino acid sequence along the bundlemer periphery, we use specific amino acid side chains, including non-natural ‘click’ chemistry functionalities, to conjugate moieties into a desired pattern, enabling the creation of a wide variety of hybrid nanomaterials.

• Research Organization: Univ. of Delaware, Newark, DE (United States)
• Sponsoring Organization: Delaware IDeA Network of Biomedical Research Excellence; National Institute of Standards and Technology (NIST); National Institutes of Health (NIH); National Science Foundation (NSF); USDOE Office of Science (SC), Basic Energy Sciences (BES); USDOE Office of Science (SC), Basic Energy Sciences (BES). Materials Sciences & Engineering Division
• Grant/Contract Number: SC0019282; SC0019355
• OSTI ID: 1633855
• Alternate ID(s): OSTI ID: 1735719; OSTI ID: 1735729
• Journal Information: Nature (London), Journal Name: Nature (London) Journal Issue: 7780 Vol. 574; ISSN 0028-0836
• Publisher: Nature Publishing Group
• Country of Publication: United States
• Language: English

Related Subjects

36 MATERIALS SCIENCE
Bioinspired materials
Chemical engineering
Molecular self-assembly
Peptides
Polymers
Self-assembly
Supramolecular polymers
bundlemer
coiled coil
peptides
self-assembly