PROPHENINS: PROLINE-RICH ANTIMICROBIAL PEPTIDES WITH REPETITIVE DECAMER SEQUENCE
UCLA Technology Available For Licensing

Prophenins belong to a new class of antimicrobial peptides discovered in mammalian white blood cells. First isolated from porcine leukocytes, prophenins display exceptionally strong endotoxin (LPS) binding activity as well as antimicrobial activity. The potential of prophenins over other LPS-binding peptides and proteins lies in their small size and their simple but unique structure, composed of repeating decameric elements. In vitro experiments indicate that prophenins have over 60 times greater affinity for LPS than polymyxin B sulfate. Thus, these peptides show promise as a new class of potent antibiotics for gram-negative bacterial infections.

The term prophenin derives from its composition, which is rich in proline (~50%) and phenylalanine (~20%). The protein sequence consists of repeating proline-rich decamers. Binding assays indicate that even an individual decamer subunit has LPS-binding activity at least equivalent to that of polymyxin B. In vitro results show that the LPS-binding properties of the holoprotein are more than the sum of its parts, but even the "parts" show enough anti-LPS activity to make them potentially useful antibiotics.

Reference: UCLA Case No. 1994-518 US Patent Number: 5,889,152
5,804,553
5,633,229

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availability, please contact the following UCLA office:

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Los Angeles, CA 90095-7231
Tel: 310-794-0558 Fax: 310-794-0638
email: ncd@research.ucla.edu
Lead Inventor: Robert Lehrer

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