Astexin peptides
AssigneeThe Trustees of Princeton University
InventorsA. James Link, Mikhail O. Maksimov
Life of this patent
Estimating the term…
Abstract
Provided are astexin-1, astexin-2 and astexin-3 lasso peptides, which are based on sequences identified in Asticaccaulis excentricus, and methods of making and using same. Astexin-1 is highly polar, in contrast to many lasso peptides that are primarily hydrophobic, and has modest antimicrobial activity against Caulobacter crescentus, a bacterium related to Asticaccaulis excentricus. The solution structure of astexin-1 was determined, revealing a unique topology that is stabilized by hydrogen bonding between segments of the peptide. Astexins-2 and -3 are intracellular lasso peptides.
Claims18
A substantially purified Astexin-3 peptide comprising the amino acid sequence GPTPMVGLDSVSGQYWDQHAPLAD (SEQ ID NO:7);
- wherein the glycine residue (G) at position 1 is covalently bound to the aspartic acid residue (D) at position 9, thereby generating a lassoed peptide.
An Astexin-3 fusion protein comprising the amino acid sequence GPTPMVGLDSVSGQYWDQHAPLAD (SEQ ID NO:7) and a second protein moiety, wherein the N-terminus of the second protein moiety is linked via a peptide bond to the C-terminus of SEQ ID NO:7.
A substantially purified Astexin-2 peptide comprising the amino acid sequence GLTQIQALDDSVSGQFRDQLGLSAD (SEQ ID NO:5) wherein the glycine residue (G) at position 1 is covalently bound to the aspartic acid residue (D) at position 9, thereby generating a lassoed peptide.
An Astexin-2 fusion protein comprising the amino acid sequence GLTQIQALDDSVSGQFRDQLGLSAD (SEQ ID NO:5) and a second protein moiety, wherein the N-terminus of the second protein moiety is linked via a peptide bond to the C-terminus of SEQ ID NO:5.
Dependencies are inferred from the claim text.