Cell penetrating peptides (CPP) are known for their ability to carry molecules across cell membrane. CPPs are efficient carriers of molecular cargo in micro-molar concentration and penetrate cell membrane without damage to the cell. Yet, CPP carriers are not selective and are not capable of targeted delivery unless specific modification is added into CPP structure. This modification is usually attachment of small molecule or peptide sequence targeting specific molecular receptor. Here we report the attempt to design a protocol for selective uptake of CPP that is based on peptide conformation. This protocol opens a possibility of targeting cells without molecular targets. Here we modified CPPs with collagen-like domain that allows peptide to fold into triple helix conformation. This folding process is reversible and temperature dependent. With confocal microscopy and flow cytometry we show the controlled internalization of CPP, dependent on peptide folding that is controlled with temperature. This type of controlled delivery may open the possibility of active targeting cells that does not have known molecular targets.

Peptide internalization triggered by temperature

249th National Meeting (2015)

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