Peptidic macromolecular assemblies
Inventors
Pochan, Darrin J. • Kloxin, Christopher James • SAVEN, Jeffery G. • WU, Dongdong • Villegas, Jose A. • Zhang, Huixi Violet
Assignees
Interested in licensing this patent?
MTEC can help explore whether this patent might be available for licensing for your application.
Publication Number
US-12545707-B2
Publication Date
2026-02-10
Expiration Date
Abstract
Provided is a non-natural macromolecular assembly that includes at least two peptide bundles and at least one linker moiety covalently linking the peptide bundles. The assembly may be used, for example, in liquid crystal materials and fibers.
Core Innovation
A non-natural macromolecular assembly is provided that is represented by formula (I) or formula (II), where the assembly includes peptide bundles PB1, PB2, and PB3 that are covalently linked. The peptide bundles PB1, PB2, and PB3 are same or different and each is a coiled coil based on a predetermined, customizable folded nanostructure into which the peptides of the peptide bundles intermolecularly assemble in aqueous solution. The assembly is formed so that it becomes a rigid rod chain, with the presence of SM1 and/or SM2 in assembly (II) increasing chain flexibility.
Linker moieties LM1 and LM2 covalently link the peptide bundles PB1, PB2, and PB3, and additional linker moieties SM1 and SM2 also contain spacer moieties. SM1 and SM2 covalently link the peptide bundles PB1, PB2, and PB3 and each of LM1, LM2, SM1, and SM2 contains at least one chemical group or moiety that is not found in proteins in nature. The assembly includes integer n from 0 to 2,000 or more, where at least 2 and up to 13 peptides comprise each peptide bundle, and each peptide contains 7 to 100 amino acids with one or more amino acids not found in nature.
The described macromolecular assemblies are non-natural and peptide-bundle-based, with the coiled coil peptide bundles forming rigid rod chains through the described covalent linking and spacer-containing linker moieties. In embodiments, spacer-containing linkers may include non-natural spacer moieties and inorganic nanoparticles that enable tuning of assembly rigidity and flexibility, and can support formation of 1-D, 2-D, or 3-D materials.
Claims Coverage
The independent claim recites a non-natural macromolecular assembly defined by formulas (I) and (II), comprising peptide bundles PB1/PB2/PB3 covalently linked by linker moieties LM1/LM2 and spacer-containing linker moieties SM1/SM2, and characterized as rigid rod chains with prescribed coiled-coil bundle assembly in aqueous solution. Dependent claim coverage introduces additional constraints on sequence uniformity, covalent linkage chemistry, spacer incorporation of inorganic nanoparticles, one-dimensional assembly characterization, and a specific spacer structure with an approximate molecular weight.
Rigid rod chain assembly from three peptide bundles linked by linker and spacer linker moieties
A non-natural macromolecular assembly represented by formula (I) or formula (II), wherein PB1, PB2, and PB3 are peptide bundles that are the same or different, LM1 and LM2 covalently link the peptide bundles, and SM1 and SM2 covalently link the peptide bundles while also containing spacer moieties; n is an integer from 0 to 2,000 or more; at least 2 and up to 13 peptides comprise each peptide bundle; each peptide contains 7 to 100 amino acids with one or more amino acids not found in nature; PB1, PB2, and PB3 are coiled coil based on a predetermined, customizable folded nanostructure that assembles in aqueous solution; LM1, LM2, SM1, and SM2 each contain at least one chemical group or moiety not found in proteins in nature; and the macromolecular assemblies (I) and (II) are rigid rod chains with SM1 and/or SM2 increasing chain flexibility in assembly (II).
Sequence-uniform peptide bundle constituent limitation
The non-natural macromolecular assembly where, within each peptide bundle, all constituent peptides share the same sequence.
Specific covalent chemistry for forming linker moieties via thiol-maleimide or azide-alkyne reactions
The non-natural macromolecular assembly where at least one of LM1 or LM2 is formed via a covalent reaction between thiol and maleimide groups or between azide and alkyne groups.
Inorganic nanoparticle within the spacer moiety of the spacer linker
The non-natural macromolecular assembly where the spacer moiety of SM1 or SM2 includes an inorganic nanoparticle.
One-dimensional macromolecular assembly characterization
The non-natural one-dimensional macromolecular assembly as defined by claim 1.
Spacer structure constraint with approximate molecular weight for SM1/SM2
The non-natural macromolecular assembly where at least one spacer moiety of SM1 and SM2 has the structure shown in the embedded image, with MW approximately 20,000.
Overall claim coverage centers on a rigid rod chain non-natural macromolecular assembly formed from three coiled-coil peptide bundles covalently linked by linker moieties and spacer-containing linker moieties, with prescribed non-natural chemical groups and peptide content; dependent claims narrow this by imposing peptide sequence uniformity, specifying thiol-maleimide or azide-alkyne covalent linkage chemistry, incorporating inorganic nanoparticles in the spacer moiety, limiting characterization to a one-dimensional assembly, and constraining spacer structure and approximate MW.
Stated Advantages
Enables formation of rigid rod chains from coiled-coil peptide bundles linked by linker moieties and spacer-containing linker moieties.
Presence of SM1 and/or SM2 in assembly (II) may increase chain flexibility.
Spacer-containing linkers and inorganic nanoparticles enable tuning of assembly rigidity/flexibility and support formation of 1-D, 2-D, or 3-D materials.
Documented Applications
Formation of 1-D, 2-D, or 3-D materials, including ultra-rigid rod polymers, semiflexible or kinked chains, temperature-reversible hydrogels, and liquid crystal phases.
Inorganic nanoparticle templated 1-D/2-D/3-D patterns and networks.
Interested in licensing this patent?