Design and validation of anti-inflammatory peptides from human parotid secretory protein

C. Geetha, S. G. Venkatesh, L. Bingle, C. D. Bingle, S. U. Gorr

Research output: Contribution to journalArticlepeer-review

36 Scopus citations


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 TNFα 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.

Original languageEnglish (US)
Pages (from-to)149-153
Number of pages5
JournalJournal of dental research
Issue number2
StatePublished - Feb 2005


  • C20orf70
  • Cationic peptides
  • Endotoxin
  • Inflammation
  • Lipopolysaccharide
  • Saliva


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