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© Research
Publication : Journal of proteomics

Laser desorption ionization mass spectrometry of protein tryptic digests on nanostructured silicon plates.

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Journal of proteomics - 03 Apr 2012

Dupré M, Coffinier Y, Boukherroub R, Cantel S, Martinez J, Enjalbal C,

Link to Pubmed [PMID] – 22282018

Link to DOI [DOI] – 10.1016/j.jprot.2011.12.039

J Proteomics 2012 Apr; 75(7): 1973-90

We report on the simple application of a new nanostructured silicon (NanoSi) substrate as laser desorption/ionization (LDI)-promoting surface for high-throughput identification of protein tryptic digests by a rapid MS profiling and subsequent MS/MS analysis. The NanoSi substrate is easily prepared by chemical etching of crystalline silicon in NH(4)F/HNO(3)/AgNO(3) aqueous solution. To assess the LDI performances in terms of sensitivity, repeatability and robustness, the detection of small synthetic peptides (380-1700Da) was investigated. Moreover, peptide sequencing was tackled. Various tryptic synthetic peptide mixtures were first characterized in MS and MS/MS experiments carried out on a single deposit. Having illustrated the capability to achieve peptide detection and sequencing on these ionizing surfaces in the same run, protein tryptic digests from Cytochrome C, β-Casein, BSA and Fibrinogen were then analyzed in the femtomolar range (from 50 fmol for Cytochrome C down to 2 fmol for Fibrinogen). Comparison of the NanoSi MS and MS/MS data with those obtained with sample conditioned in organic matrix demonstrated a great behavior for low mass responses. We demonstrated the capability of LDI on NanoSi to be a complementary method to MALDI peptide mass fingerprinting ensuring determination of peptide molecular weights and sequences for more efficient protein database searches.

https://pubmed.ncbi.nlm.nih.gov/22282018