TY - JOUR
T1 - Formulating tumor-homing peptides as regular nanoparticles enhances receptor-mediated cell penetrability
AU - Xu, Zhikun
AU - Unzueta, Ugutz
AU - Roldán, Mónica
AU - Mangues, Ramón
AU - Sánchez-Chardi, Alejandro
AU - Ferrer-Miralles, Neus
AU - Villaverde, Antonio
AU - Vázquez, Esther
PY - 2015/9/1
Y1 - 2015/9/1
N2 - © 2015 Elsevier B.V. All rights reserved. Abstract Homing peptides are exploited in nanomedicine to functionalize either free drugs or nanostructured materials used as drug carriers. However, the influence of multivalent versus monovalent peptide presentation on the interaction with the receptor and on the consequent intracellular delivery of the associated cargo remains poorly explored. By using a tumor-homing peptide (T22) with regulatable self-assembling properties we have investigated here if its display in a either a monomeric form or as multimeric, self-assembled protein nanoparticles might determine the efficacy of receptor-mediated penetrability into target cells. This has been monitored by using a fluorescent cargo protein (iRFP), which when fused to the homing peptide acts as convenient reporter. The results indicate that the nanoparticulate protein versions are significantly more efficient in mediating receptor-dependent uptake than their unassembled counterparts. These finding stresses an additional benefit of nanostructured materials based on repetitive building blocks, regarding the multivalent presentation of cell ligands that facilitate cell penetration in drug delivery applications.
AB - © 2015 Elsevier B.V. All rights reserved. Abstract Homing peptides are exploited in nanomedicine to functionalize either free drugs or nanostructured materials used as drug carriers. However, the influence of multivalent versus monovalent peptide presentation on the interaction with the receptor and on the consequent intracellular delivery of the associated cargo remains poorly explored. By using a tumor-homing peptide (T22) with regulatable self-assembling properties we have investigated here if its display in a either a monomeric form or as multimeric, self-assembled protein nanoparticles might determine the efficacy of receptor-mediated penetrability into target cells. This has been monitored by using a fluorescent cargo protein (iRFP), which when fused to the homing peptide acts as convenient reporter. The results indicate that the nanoparticulate protein versions are significantly more efficient in mediating receptor-dependent uptake than their unassembled counterparts. These finding stresses an additional benefit of nanostructured materials based on repetitive building blocks, regarding the multivalent presentation of cell ligands that facilitate cell penetration in drug delivery applications.
KW - Biomaterials
KW - Biomimetic
KW - Nanoparticles
KW - Protein materials
UR - https://ddd.uab.cat/record/132808
U2 - https://doi.org/10.1016/j.matlet.2015.04.055
DO - https://doi.org/10.1016/j.matlet.2015.04.055
M3 - Article
VL - 154
SP - 140
EP - 143
M1 - 18798
ER -