MALDI-TOF mass spectrometry: a powerful tool to study the internalization of cell-penetrating peptides.

S. Aubry (1, 2) , B. Aussedat (1, 2) , D. Delaroche (1, 2) , J. Chen-Yu (1, 2) , G. Bolbach (2, 1) , S. Lavielle (1, 2) , G. Chassaing (1, 2) , S. Sagan (1, 2) , F. Burlina (1, 2)

1 UPMC - Université Pierre et Marie Curie - Paris 6
2 FR 2769 - Chimie Moléculaire de Paris Centre

This review summarizes the contribution of MALDI-TOF mass spectrometry in the study of cell-penetrating peptide (CPP) internalization in eukaryote cells. This technique was used to measure the efficiency of cell-penetrating peptide cellular uptake and cargo delivery and to analyze carrier and cargo intracellular degradation. The impact of thiol-containing membrane proteins on the internalization of CPP-cargo disulfide conjugates was also evaluated by combining MALDI-TOF MS with simple thiol-specific reactions. This highlighted the formation of cross-linked species to cell-surface proteins that either remained trapped in the cell membrane or led to intracellular delivery. MALDI-TOF MS is thus a powerful tool to dissect CPP internalization mechanisms.

Domaines: Chimie organique

S. Aubry, B. Aussedat, D. Delaroche, J. Chen-Yu, G. Bolbach, et al.. MALDI-TOF mass spectrometry: a powerful tool to study the internalization of cell-penetrating peptides.. BBA - Biochimica et Biophysica Acta, 2010, 1798 ((12)), pp.2182-9. ⟨10.1016/j.bbamem.2009.11.011⟩. ⟨hal-00578947⟩