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Multivalent presentation of the cell-penetrating peptide nona-arginine on a linear scaffold strongly increases its membrane-perturbing capacity.
Chakrabarti A, Witsenburg JJ, Sinzinger MD, Richter M, Wallbrecher R, Cluitmans JC, Verdurmen WP, Tanis S, Adjobo-Hermans MJ, Rademann J, Brock R. Chakrabarti A, et al. Biochim Biophys Acta. 2014 Dec;1838(12):3097-106. doi: 10.1016/j.bbamem.2014.08.001. Epub 2014 Aug 7. Biochim Biophys Acta. 2014. PMID: 25109936 Free article.
Membrane permeation of arginine-rich cell-penetrating peptides independent of transmembrane potential as a function of lipid composition and membrane fluidity.
Wallbrecher R, Ackels T, Olea RA, Klein MJ, Caillon L, Schiller J, Bovée-Geurts PH, van Kuppevelt TH, Ulrich AS, Spehr M, Adjobo-Hermans MJW, Brock R. Wallbrecher R, et al. J Control Release. 2017 Jun 28;256:68-78. doi: 10.1016/j.jconrel.2017.04.013. Epub 2017 Apr 12. J Control Release. 2017. PMID: 28411183 Free article.
48 results