TY - JOUR
T1 - Guiding plant virus particles to integrin-displaying cells
AU - Hovlid, Marisa L.
AU - Steinmetz, Nicole F.
AU - Laufer, Burkhardt
AU - Lau, Jolene L.
AU - Kuzelka, Jane
AU - Wang, Qian
AU - Hyypiä, Timo
AU - Nemerow, Glen R.
AU - Kessler, Horst
AU - Manchester, Marianne
AU - Finn, M. G.
PY - 2012/6/12
Y1 - 2012/6/12
N2 - Viral nanoparticles (VNPs) are structurally regular, highly stable, tunable nanomaterials that can be conveniently produced in high yields. Unmodified VNPs from plants and bacteria generally do not show tissue specificity or high selectivity in binding to or entry into mammalian cells. They are, however, malleable by both genetic and chemical means, making them useful scaffolds for the display of large numbers of cell- and tissue-targeting ligands, imaging moieties, and/or therapeutic agents in a well-defined manner. Capitalizing on this attribute, we modified the genetic sequence of the Cowpea mosaic virus (CPMV) coat protein to display an RGD oligopeptide sequence derived from human adenovirus type 2 (HAdV-2). Concurrently, wild-type CPMV was modified via NHS acylation and Cu(i)-catalyzed azide-alkyne cycloaddition (CuAAC) chemistry to attach an integrin-binding cyclic RGD peptide. Both types of particles showed strong and selective affinity for several different cancer cell lines that express RGD-binding integrin receptors.
AB - Viral nanoparticles (VNPs) are structurally regular, highly stable, tunable nanomaterials that can be conveniently produced in high yields. Unmodified VNPs from plants and bacteria generally do not show tissue specificity or high selectivity in binding to or entry into mammalian cells. They are, however, malleable by both genetic and chemical means, making them useful scaffolds for the display of large numbers of cell- and tissue-targeting ligands, imaging moieties, and/or therapeutic agents in a well-defined manner. Capitalizing on this attribute, we modified the genetic sequence of the Cowpea mosaic virus (CPMV) coat protein to display an RGD oligopeptide sequence derived from human adenovirus type 2 (HAdV-2). Concurrently, wild-type CPMV was modified via NHS acylation and Cu(i)-catalyzed azide-alkyne cycloaddition (CuAAC) chemistry to attach an integrin-binding cyclic RGD peptide. Both types of particles showed strong and selective affinity for several different cancer cell lines that express RGD-binding integrin receptors.
UR - http://www.scopus.com/inward/record.url?scp=84867865404&partnerID=8YFLogxK
U2 - 10.1039/c2nr30571b
DO - 10.1039/c2nr30571b
M3 - Article
C2 - 22585108
AN - SCOPUS:84867865404
SN - 2040-3364
VL - 4
SP - 3698
EP - 3705
JO - Nanoscale
JF - Nanoscale
IS - 12
ER -
