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Purification of Biotinylated Cell Surface Proteins from Rhipicephalus microplus Epithelial Gut Cells
Published on: July 23, 2017
(1)H, (15)N and (13)C assignments of the Rhipicephalus (Boophilus) microplus anti-microbial peptide microplusin
Carlos A Rezende1, Fernanda D Silva, Sirlei Daffre
1Instituto de Bioquímica Médica, CCS, Universidade Federal do Rio de Janeiro, Av. Brigadeiro Trompowiski s/n, Rio de Janeiro, RJ, 21941-590, Brazil.
Abstract:
Microplusin, a Rhipicephalus (Boophilus) microplus anti-microbial peptide (AMP) is the first member of a new family of cysteine-rich AMPs with histidine-rich regions at the N- and C-termini, which is being fully characterized by biophysical and biochemical methods. Here we report the NMR resonance assignments for (1)H, (15)N, and (13)C nuclei in the backbone and side chains of the microplusin as basis for further studies of structure, backbone dynamics and interactions mapping.
Insights
Researchers characterized microplusin, a novel antimicrobial peptide from the Rhipicephalus (Boophilus) microplus tick. This study provides NMR assignments for microplusin, enabling future structural and dynamic analyses.
Area of Science:
- Biochemistry
- Structural Biology
- Antimicrobial Peptides
Background:
- Microplusin is a novel antimicrobial peptide (AMP) identified in the Rhipicephalus (Boophilus) microplus tick.
- It represents the first characterized member of a new family of cysteine-rich AMPs.
- This peptide family features distinctive histidine-rich regions at both the N- and C-termini.
Purpose of the Study:
- To report the complete NMR resonance assignments for microplusin.
- To establish a foundation for detailed structural and dynamic studies of this unique AMP.
- To enable future investigations into microplusin's interaction mechanisms.
Main Methods:
- Nuclear Magnetic Resonance (NMR) spectroscopy was employed.
- Resonance assignments were determined for 1H, 15N, and 13C nuclei.
- Assignments covered both the backbone and side chains of the microplusin peptide.
Main Results:
- Complete 1H, 15N, and 13C NMR resonance assignments for microplusin were successfully obtained.
- These assignments provide crucial data for understanding the peptide's structural characteristics.
- The data serves as a basis for further biophysical and biochemical characterization.
Conclusions:
- The reported NMR assignments are essential for elucidating the three-dimensional structure of microplusin.
- This work facilitates future studies on the backbone dynamics and interaction mapping of microplusin.
- Understanding microplusin's structure and dynamics is key to exploring its potential as an antimicrobial agent.

