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- W1965467605 endingPage "607" @default.
- W1965467605 startingPage "598" @default.
- W1965467605 abstract "Peptides including HIV-1 Tat peptide and oligoarginines represent arginine-rich membrane-permeable vectors that attain efficient intracellular delivery of bioactive molecules. The importance of the arginine residues or their guanidino functions is now appreciated for efficient internalization of the Tat peptide, and based on this, various novel arginine/guanidino-rich vectors have now been developed. However, molecular detail of their method(s) of internalization are still debated. This review summarizes our current understandings of endocytic and non-endocytic aspects of internalization of arginine-rich peptide vectors. We highlight the possibility of simultaneous employment of multiple internalization pathways, the contribution of which is dependent on a number of factors. Similarities and dissimilarities among the internalization methods of typical peptide vectors and other guanidino-rich vectors including branched-chain, β-peptide, and sugar-based vectors, are also discussed." @default.
- W1965467605 created "2016-06-24" @default.
- W1965467605 creator A5000566593 @default.
- W1965467605 creator A5008029220 @default.
- W1965467605 creator A5040691390 @default.
- W1965467605 creator A5047418888 @default.
- W1965467605 date "2008-03-01" @default.
- W1965467605 modified "2023-10-11" @default.
- W1965467605 title "Methodological and cellular aspects that govern the internalization mechanisms of arginine-rich cell-penetrating peptides" @default.
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- W1965467605 doi "https://doi.org/10.1016/j.addr.2007.10.006" @default.
- W1965467605 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/18045727" @default.
- W1965467605 hasPublicationYear "2008" @default.