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Engineering Biomimetic Peptides for Targeted Drug Delivery--Efrosini Kokkoli
Pages 139-148

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From page 139...
... polymer strands attached to a fraction of hydrophilic lipid headgroups. These PEG chains form a polymer brush on the surface of the liposome that, through steric repulsion, resists protein adhesion, and therefore clearance by the reticuloendothelial system (RES)
From page 140...
... , which specifically binds to FGFR-expressing cells, such as melanoma, breast cancer, and prostate cancer cells; the pentapeptide yIGSR, derived from the glycoprotein laminin, which has been shown to bind with high affinity to the laminin receptor over-expressed in human tumor cells; the NGR and APRGP peptides, which have been used as potential targeting moieties against tumor vasculature; and others (Pangburn et al., 2009)
From page 141...
... In this example, the self-assembly of the hydrophobic tails of the peptide-amphiphiles align the peptide strands and induce and/or stabilize the three-dimensional structure of the peptide headgroup into triple helices, giving rise to protein-like molecular architectures (Figure 1)
From page 142...
... The RGD sequence, located in the 10th type III repeat of the fibronectin molecule, which was originally identified as a cellbinding site in the extracellular matrix protein fibronectin, has been used as a targeting moiety on numerous occasions. Although RGD has been used with some success as a targeting moiety against integrins, it does not have the same adhesive properties as native fibronectin (Akiyama et al., 1995; Garcia et al., 2002; yang et al., 2001)
From page 143...
... . Although various targeting moieties incorporating both the RGD and PHSRN sequences have been tested, most of these designs did not achieve the cell-adhesion densities supported by native fibronectin over similar time scales (Aucoin et al., 2002; Benoit and Anseth, 2005; kao, 1999; kim et al., 2002; Petrie et al., 2006)
From page 144...
... Although previous attempts had been made to match the distance between the RGD and PHSRN sequences, they did not pay particular attention to the hydro philicity/hydrophobicity of the linker. Mardilovich and kokkoli's efforts culminated in the design of a biomimetic peptide, named PR_b, which is now well established as a close mimic of the α5β1 binding site in fibronectin and is a highly effective and specific targeting peptide (Mardilovich et al., 2006)
From page 145...
... 1990. Characterization of a synthetic peptide from type IV collagen that promotes melanoma cell adhesion, spreading, and motility.
From page 146...
... 2006. Integrin specificity and enhanced cellular activities associated with surfaces presenting a recombinant fibronectin fragment com pared to RGD supports.
From page 147...
... Journal of the American Chemical Society 120(39)


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