Secondary conformational conversion is involved in glycosaminoglycans‐mediated cellular uptake of the cationic cell‐penetrating peptide PACAP | Zendy

Tchoumi Neree Armelle | Zendy; Nguyen Phuong Trang | Zendy; Chatenet David | Zendy; Fournier Alain | Zendy; Bourgault Steve | Zendy

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Secondary conformational conversion is involved in glycosaminoglycans‐mediated cellular uptake of the cationic cell‐penetrating peptide PACAP

Author(s) -

Tchoumi Neree Armelle,

Nguyen Phuong Trang,

Chatenet David,

Fournier Alain,

Bourgault Steve

Publication year - 2014

Publication title -

febs letters

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.593

H-Index - 257

eISSN - 1873-3468

pISSN - 0014-5793

DOI - 10.1016/j.febslet.2014.10.029

Subject(s) - internalization , glycosaminoglycan , chemistry , peptide , microbiology and biotechnology , cationic polymerization , cell penetrating peptide , cell , biochemistry , biophysics , biology , organic chemistry

Glycosaminoglycans (GAGs) contribute to the cellular uptake of cationic cell‐penetrating peptides (CPPs). However, molecular details about the contributions of GAGs in CPP internalization remain unclear. In this study, we examined the cellular uptake mechanism of the arginine‐rich CPP pituitary adenylate‐cyclase‐activating polypeptide (PACAP). We observed that the uptake efficacy of PACAP is dependent on the expression of cell surface GAGs. As the binding of PACAP to sulfated GAGs induced a random coil‐to‐α‐helix conformational conversion, we investigated the role of the helical formation in PACAP internalization. Whereas this secondary structure was not crucial for efficient internalization in GAGs‐deficient cells, PACAP α‐helix was essential for GAGs‐dependent uptake.

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