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Publication Number
US-12458692-B2
Publication Date
2025-11-04
Expiration Date
Abstract
The present disclosure describes a peptide scaffold for producing vaccines. The peptide scaffold includes a peptide that self-assembles into a hapten carrier (hC) that includes amphipathic alpha-helices. The peptide includes heptad repeats following a specific pattern. The hC further includes hapten or an agent conjugated to it, and optionally the hC includes one or more T-cell epitopes at the N- and/or C-terminus of the one or more amphipathic alpha-helices. The present disclosure also describes compositions including immunogenic compositions including the hapten-hC or agent-hC conjugate.
Core Innovation
The invention describes a fully synthetic vaccine peptide scaffold built from monomer peptides that include repeating heptad sequences. Each heptad has an amphipathic alpha-helical heptad pattern, and multiple heptads are combined into a repeating peptide pattern. The resulting peptides self-assemble into hapten carriers, including hexameric hapten carriers (HhC), that provide hapten carrier structure for subsequent conjugation.
The scaffold includes hapten conjugation sites that are optimized at a defined residue position, with coupling performed through a y residue that corresponds to lysine (K) or arginine (R). The design requires at least one K residue in the peptide and specifies that K is the only residue used for coupling a hapten. Carrier-stabilized hapten conjugates are described as constructs that can include B-cell hapten conjugates.
The invention further describes optional CD4+/T-cell epitopes positioned at helix N-termini and/or C-termini of the amphipathic alpha-helices, to provide T-cell help and support immune responses. Immunogenic compositions are described using pharmaceutically acceptable excipients and adjuvants, including monophosphoryl lipid A (MPL) and MPL-squalene. The disclosed rationale includes confirmation of scaffold stability and self-assembly, and immunogenicity characterization using prime-boost immunization studies.
Claims Coverage
The independent claim covers a peptide scaffold defined by a repeating heptad sequence pattern, with specific amino-acid assignments, a limited repeat number, and a restriction that hapten coupling occurs only through lysine (K). It further requires the presence of at least one K residue and includes coupling specificity as a central inventive constraint, resulting in hapten carrier constructs formed via self-assembly.
Repeating heptad amphipathic pattern peptide scaffold
A peptide comprising two or more heptads, wherein the heptad has the amino acid sequence hwxhxyz (SEQ ID NO: 19), and the peptide comprises the amino acid sequence pattern (hwxhxyz)n (SEQ ID NO: 20), with h=I, w=R, x=S or G, y=K or R, z=E, and n=2 to 4.
Hapten coupling restricted to lysine only
There is at least one K residue in the peptide and K is the only residue used for coupling a hapten.
Together, the claim coverage centers on a self-assembling, fully synthetic heptad-repeat peptide scaffold with a defined amphipathic alpha-helical pattern, limited repeat number, and a strict hapten-coupling rule requiring lysine (K) to be the only coupling residue.
Stated Advantages
Induces robust immune responses.
Enhances immunogenicity of a hapten.
Documented Applications
Vaccine compositions and immunogenicity characterization, including prime-boost immunization studies.
Pharmaceutical compositions formulated with pharmaceutically acceptable excipients and described adjuvants such as MPL and MPL-squalene.
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