Journal
FEBS LETTERS
Volume 588, Issue 24, Pages 4590-4596Publisher
WILEY
DOI: 10.1016/j.febslet.2014.10.029
Keywords
Cell-penetrating peptide; Glycosaminoglycan; alpha-Helix; Pituitary adenylate cyclase-activating polypeptide; Cellular uptake
Funding
- Natural Sciences and Engineering Research Council of Canada
- Canadian Institutes of Health Research
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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-alpha-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 alpha-helix was essential for GAGs-dependent uptake. (C) 2014 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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