Matrix scaffold with antimicrobial activity

• US 8,969,290 B2
• Filed: 06/26/2013
• Issued: 03/03/2015
• Est. Priority Date: 06/26/2012
• Status: Active Grant

• Current Assignee: Worcester Polytechnic Institute
• Original Assignee: Worcester Polytechnic Institute
• Inventors: Rolle, Marsha, Prifti, Fioleda, Malcuit, Chris, Camesano, Terri Anne, Dominko, Tanja, Kole, Denis
• Primary Examiner(s): Acevedo, James H Alstrum
• Assistant Examiner(s): MARTINEZ, TARA L
• Application Number:
  US13/928,245
• Publication Number:
  US 20130345118A1
• Time in Patent Office: 615 Days
• Field of Search: 514/3.2, 514/2.3, 530/350
• US Class Current: 514/2.3
• CPC Class Codes: A61L 2300/404 Biocides, antimicrobial agents, antiseptic agents
• CPC Class Codes: A61L 27/54 Biologically active materials, e.g. therapeutic substances A61L27/227 takes precedence
• CPC Class Codes: C07K 14/4723 Cationic antimicrobial peptides, e.g. defensins
• CPC Class Codes: C07K 14/78 Connective tissue peptides, e.g. collagen, elastin, laminin, fibronectin, vitronectin or cold insoluble globulin [CIG]
• CPC Class Codes: C07K 2319/00 Fusion polypeptide
• CPC Class Codes: C12N 15/62 DNA sequences coding for fusion proteins

Abstract

The invention provides a scaffold of extracellular matrix polymers with recombinant chimeric peptides tethered thereto. The invention also provides recombinant chimeric peptides of antimicrobial peptides and extracellular matrix binding domains. The invention also provides methods for treating chronic wounds using the scaffold and/or recombinant chimeric peptides.

Claims

1. A chimeric peptide comprising

MKTQRDGHSLGRWSLVLLLLGLVMPLAIIAQVLSYKEAVLRAIDGINQRSSDANLYRLL DLDPRPTMDGDPDTPKPVSFTVKETVCPRTTQQSPEDCDFKKDGLVKRCMGTVTLNQA RGSFDISCDKDNKRFALLGDFFRKSKEKIGKEFKRIVQRIKDFLRNLVPRTES (SEQ ID NO:

4) and a collagen binding domain selected from the group consisting of TKKTLRT (SEQ ID NO;

     5) and CQDSETGTFY (SEQ ID NO;

     6), attached to the C-terminal end of SEQ ID NO;

4 via a linker sequence comprising five aspartic acid residues, two lysine residues and a tyrosine residue.

2. The chimeric peptide of claim 1, wherein the collagen binding domain is SEQ ID NO:

5.

3. The chimeric peptide of claim 1, wherein the collagen binding domain is SEQ ID NO:

6.