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US 2004/0024176 A1Published application
Cyclic peptide tube
AssigneeThe Scripps Research Institute
InventorReza M. Ghadiri
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AssigneeThe Scripps Research Institute
InventorReza M. Ghadiri
Estimating the term…
Cyclic homodetic peptides having a repeating D-L-chirality motif are shown to have a stable disk conformation with the amino acid side chains extending radially outward and the carbonyl and amino groups extending axially upward or downward. Such cyclic peptides can be employed as subunits in the assembly of molecular tubes. Cyclic peptides having a repeating D-L-chirality motif and lacking mutually repulsive side-chains are shown to stack atop one another in an anti-parallel fashion and are shown to be held together by the formation of β-sheet hydrogen bonding. The stacked cyclic peptides form a molecular tube having a central channel. The diameter of the channel is determined by the size cyclic peptide. If the cyclic peptide includes ionizable amino acid residues, e.g. glutamic acid or lysine, assembly and disassembly of the molecular tubes can be controlled by varying the pH. If the cyclic peptide includes hydrophobic amino acid residues, the molecular tube will insert into a lipid membrane. In such instances, the molecular tube provides a transmembrane channel. The channel can be gated or ungated. Molecular tubes can be terminated with a terminal cyclic peptide having methylated amino groups in one orientation. Molecular tubes may be employed as drug carriers, molecular sieves, reaction vessels, membrane channels, and other uses.
A cyclic homodetic peptide comprising an amino acid sequence having an even number of amino acid residues, having a length between 6 and 16 amino acid residues, having a repeating D-L-chirality motif, and lacking glycine.
A molecular tube comprising:
A method for assembling a molecular tube comprising the following step:
A cyclic homodetic peptide comprising a glycine-free amino acid sequence having an even number of amino acid residues, having a length of 6 to 16 amino acid residues, having a repeating D-L-chirality motif, and blocked backbone nitrogen for one of the chirality moieties thereof.
A tubular peptide comprising a ring structure constituted by antiparallel stacks of paired, hydrogen bonded peptide ring subunits at least one of which is devoid of hydrogen bond donors on one face thereof.
A crystalline, continuously channeled lattice constituted by ring structures that include antiparallel stacks of paired, hydrogen bonded peptide ring subunits at least one of such subunits being devoid of hydrogen bond donors on one face thereof.
A cyclic peptide oligomer having a ring structure in which hydrogen bond donors are present on one face thereof and hydrogen bond donors are absent on the other face thereof;
A self-assembled peptide nanotube capped at at least one end thereof by a cyclic peptide having a ring structure with hydrogen bond donors on one face of the ring structure and devoid of hydrogen bond donors on the other face of the ring structure.
A method of making a discrete cylindrical peptide oligomer comprising the steps of introducing an oligomeric peptide constituting at least six and no more than 16 amino acid residues of alternating D-L-chirality, and having only blocked amino groups in one of the chiral motifs thereof, in a nonpolar organic solvent, combining the resulting solution with 2-(1H-benzotriazol-1-yl) -1,1,3,3-tetramethyluronium tetrafluoroborate, 1-hydroxybenzotriazole and diisopropylethylamine to form an admixture, and maintaining the formed admixture at about 5° C. for about 12 hours.
Dependencies are inferred from the claim text.