The patent badge is an abbreviated version of the USPTO patent document. The patent badge does contain a link to the full patent document.

The patent badge is an abbreviated version of the USPTO patent document. The patent badge covers the following: Patent number, Date patent was issued, Date patent was filed, Title of the patent, Applicant, Inventor, Assignee, Attorney firm, Primary examiner, Assistant examiner, CPCs, and Abstract. The patent badge does contain a link to the full patent document (in Adobe Acrobat format, aka pdf). To download or print any patent click here.

Date of Patent:
Nov. 11, 2014

Filed:

Mar. 26, 2010
Applicants:

John M. Tomich, Manhattan, KS (US);

Takeo Iwamoto, Manhattan, KS (US);

Yasuaki Hiromasa, Manhattan, KS (US);

Sushanth Gudlur, Manhattan, KS (US);

Inventors:

John M. Tomich, Manhattan, KS (US);

Takeo Iwamoto, Manhattan, KS (US);

Yasuaki Hiromasa, Manhattan, KS (US);

Sushanth Gudlur, Manhattan, KS (US);

Assignee:
Attorney:
Primary Examiner:
Assistant Examiner:
Int. Cl.
CPC ...
A61K 38/08 (2006.01); A61K 38/10 (2006.01); A61K 9/107 (2006.01); A61K 9/127 (2006.01); A61K 9/51 (2006.01); A61K 47/48 (2006.01); C07K 7/02 (2006.01);
U.S. Cl.
CPC ...
A61K 9/1075 (2013.01); A61K 9/1273 (2013.01); A61K 9/5169 (2013.01); A61K 47/48038 (2013.01); A61K 47/488 (2013.01); C07K 7/02 (2013.01);
Abstract

The present invention provides branched amphipathic peptides and vesicles formed thereof. The peptides comprise a polar/positively charged C-terminal segment, a branch point, and two hydrophobic N-terminal segments extending from the branch point. The vesicles are formed using a plurality of first and second peptides, wherein the first peptide has a different chain length from the second peptide. When a plurality of the first and second peptides are mixed together, they self-assemble to form small spheres defined by a membrane consisting of an interlocking peptide network bilayer and having a liquid-receiving interior space (i.e., hollow core). In the bi-layer, the respective hydrophobic segments of the peptides form beta-sheet structures having a hydrogen bond-stabilized, anti-parallel orientation in which the opposed sequences interlock to form a zipper-like structure in three dimensions. Thus, the peptide assembly (i.e., vesicle) can be held together at reduced concentrations where lipid vesicles would breakdown.


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