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Journal of Dental Research
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Biological

Design and Validation of Anti-inflammatory Peptides from Human Parotid Secretory Protein

C. Geetha1,2, S.G. Venkatesh1,*, L. Bingle3, C.D. Bingle3 and S.-U. Gorr1,4

1 Department of Periodontics, Endodontics and Dental Hygiene, Room 209C, and
4 Department of Biochemistry and Molecular Biology, University of Louisville Health Sciences Center, School of Dentistry, Louisville, KY 40292, USA;
3 Academic Unit of Respiratory Medicine, Division of Genomic Medicine, The University of Sheffield Medical School, Royal Hallamshire Hospital, Sheffield S10 2JF, UK;

Correspondence: * corresponding author, venkatesh.srirangapatnam{at}louisville.edu

Parotid secretory protein (PSP) and palate-lung-nasal epithelium clone (PLUNC) are novel secretory proteins that are expressed in the oral cavity and upper airways. Both proteins are related to bactericidal/permeability increasing protein (BPI). Cationic peptides derived from BPI exhibit anti-inflammatory activity. To test if PSP (C20orf70 gene product) also contains anti-inflammatory peptides, we designed 3 cationic peptides based on the predicted structure of PSP and known active regions of BPI. Each peptide inhibited the lipopolysaccharide (LPS)-stimulated secretion of TNF{alpha} from RAW 264.7 macrophage cells. At 200 µg/mL, the peptide GK-7 exhibited inhibition similar to that achieved with 10 µg/mL of polymyxin B. PSP peptides directly inhibited the binding of LPS to LPS-binding protein. The cationic peptide Substance P had no inhibitory effect in these assays, confirming the specificity of the PSP peptides. These findings suggest that PSP peptides can serve as templates for the design of novel anti-inflammatory peptides.

Key Words: cationic peptides • endotoxin • inflammation • lipopolysaccharide • PLUNC • saliva • C20orf70

Journal of Dental Research, Vol. 84, No. 2, 149-153 (2005)
DOI: 10.1177/154405910508400208
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