Peptide data on the disulfide bond analysis of baculovirus produced Pfs25 by LC-MSMS

Area of Science:

• Biochemistry
• Structural Biology
• Vaccinology

Background:

• Pfs25 is a Plasmodium falciparum protein and a malaria transmission-blocking vaccine candidate.
• The protein possesses a compact and intricate structure with 22 cysteine residues, necessitating detailed structural analysis.
• Understanding disulfide bonds is critical for Pfs25's stability and function as a vaccine.

Purpose of the Study:

• To present supplementary peptide data from the disulfide bond mapping of recombinant Pfs25.
• To provide detailed information on theoretical peptides, masses, and disulfide bond linkages.
• To facilitate further research on Pfs25 structure-function relationships.

Main Methods:

• Recombinant Pfs25 produced via a baculovirus expression system.
• Enzymatic digestion of Pfs25 using trypsin/Lys-C.
• Separation of peptides by High-Performance Liquid Chromatography (HPLC).
• Analysis of peptides using mass spectrometry (MS) with MS^E fragmentation.

Main Results:

• Identification of theoretical peptides and their corresponding masses.
• Mapping of disulfide bond locations and identification of linked peptides.
• Comprehensive mass spectrometry analysis data.

Conclusions:

• The presented data provides critical insights into the disulfide bond architecture of Pfs25.
• This information is vital for the rational design and development of Pfs25-based malaria vaccines.
• The raw data is publicly available for broader scientific access and utilization.