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Screening inhibitory peptides against sphingomyelinase D from the livestock tick Rhipicephalus microplus using phage
Fernando A A Silva1, Gabriel C A Costa1, Ricardo J S Torquato1
1Departamento de Bioquímica, Escola Paulista de Medicina, Universidade de Federal de São Paulo (UNIFESP), São Paulo, SP, Brazil.
Biochimie
|June 18, 2025
Summary
Researchers identified two novel peptides that inhibit sphingomyelinase D-like protein from the cattle tick Rhipicephalus microplus. These peptide inhibitors may offer new therapeutic strategies for diseases linked to sphingomyelinase activity.
Area of Science:
- Biochemistry
- Parasitology
- Drug Discovery
Background:
- The cattle tick Rhipicephalus microplus causes significant economic losses in the livestock industry.
- A sphingomyelinase (SMase) D-like protein (RmSMase) in tick saliva is implicated in its pathogenicity.
- SMases are enzymes found in various organisms, including spiders and bacteria, and are linked to human diseases.
Purpose of the Study:
- To identify peptide inhibitors of the Rhipicephalus microplus sphingomyelinase D-like protein (RmSMase).
- To characterize the inhibitory activity and mechanism of identified peptides.
- To explore the potential therapeutic applications of these inhibitors.
Main Methods:
- Phage display technology was used to screen a peptide library against RmSMase.
- Two synthesized peptides, RWLWWLW and WLSWLW, demonstrated inhibitory activity.
- Enzyme kinetics and docking analysis were performed to elucidate the inhibition mechanism.
Main Results:
- Two peptides, RWLWWLW and WLSWLW, were identified as inhibitors of RmSMase.
- RWLWWLW exhibited competitive inhibition with a Ki of 5.35 ± 0.46 μM.
- Both peptides also inhibited bacterial SMase C from Bacillus cereus, with IC50 values of 4.99 ± 0.07 μM and 16.94 ± 8.71 μM, respectively.
Conclusions:
- This study is the first to report peptide inhibitors against tick SMase using phage display.
- The identified peptides block substrate access to the catalytic site of RmSMase.
- These novel SMase inhibitors hold potential for developing new treatments for diseases associated with SMase activity.
