Reference : Structural Polymorphism Of Two Cpp: An Important Parameter Of Activity
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
Structural Polymorphism Of Two Cpp: An Important Parameter Of Activity
Deshayes, S. [> > > >]
Decaffmeyer, Marc [Université de Liège - ULg > > Gembloux Agro-Bio Tech >]
Brasseur, Robert mailto [Université de Liège - ULg > > Gembloux Agro-Bio Tech >]
Thomas, Annick [Université de Liège - ULg > Chimie et bio-industries > Centre de Bio. Fond. - Section de Biologie moléc. et numér. >]
Biochimica et Biophysica Acta-Biomembranes
Yes (verified by ORBi)
[en] Despite numerous investigations, the important structural features of Cell
Penetrating Peptides (CPPs) remain unclear as demonstrated by the difficulties
encountered in designing new molecules. In this study, we focused our interest on
Penetratin and Transportan and several of their variants. Penetratin W48F and
Penetratin W48F/W56F exhibit a reduced and a complete lack of cellular uptake,
respectively; TP07 and TP10 present a similar cellular uptake as Transportan and
TP08, TP13 and TP15 display no or weak internalization capacity. We applied the
algorithmic method named PepLook to analyze the peptide polymorphism. The study
reveals common conformational characteristics for the CPPs and their permeable
variants: they all are polymorphic. Negative, non permeable, mutants share the
opposite feature since they are monomorphic. Finally, we support the hypothesis
that structural polymorphism may be crucial since it provides peptides with the
possibility of adapting their conformation to medium hydrophobicity and or to
partner diversity.
Researchers ; Professionals

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