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, beta-peptide, and sugar-based vectors, are also discussed.