CoChat
Sign Up
Cited by 225

The DOI matches its Crossref record.

Peptide-Based Drug-Delivery Systems in Biotechnological Applications: Recent Advances and Perspectives

Tesauro, Diego, Accardo, Antonella, Diaferia, Carlo, Milano, Vittoria, Guillon, Jean, Ronga, Luisa, Rossi, Filomena·2019·Molecules
DOI 10.3390/molecules24020351PMC PMC6359574
Open this paper in CoChat — free account

Abstract

Peptides of natural and synthetic sources are compounds operating in a wide range of biological interactions. They play a key role in biotechnological applications as both therapeutic and diagnostic tools. They are easily synthesized thanks to solid-phase peptide devices where the amino acid sequence can be exactly selected at molecular levels, by tuning the basic units. Recently, peptides achieved resounding success in drug delivery and in nanomedicine smart applications. These applications are the most significant challenge of recent decades: they can selectively deliver drugs to only pathological tissues whilst saving the other districts of the body. This specific feature allows a reduction in the drug side effects and increases the drug efficacy. In this context, peptide-based aggregates present many advantages, including biocompatibility, high drug loading capacities, chemical diversity, specific targeting, and stimuli responsive drug delivery. A dual behavior is observed: on the one hand they can fulfill a structural and bioactive role. In this review, we focus on the design and the characterization of drug delivery systems using peptide-based carriers; moreover, we will also highlight the peptide ability to self-assemble and to actively address nanosystems toward specific targets.

Overview

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Integrity signals

Registry

Crossref · 10.3390/molecules24020351

Cites

Statistics

Figures

Figure 1 Different classes of peptides can be arrange in supramolecular structures handling the self-assembling phenomena. Various morphologies can be generated according to the rational design of the primary sequence.
Figure 1 Different classes of peptides can be arrange in supramolecular structures handling the self-assembling phenomena. Various morphologies can be generated according to the rational design of the primary sequence.CC BY · PubMed Central
Figure 2 Diphenylalanine based aggregates can be applied with different biotechnological scopes, producing drug delivery systems, hydrogels matrices, supramolecular contrast agents, and fluorescent aggregates. Chemical and functional decorations (like sequences modification, incorporation of fluorescent dyes and conjugation with chelating agents and polymers) at N- and C-terminus of the primary sequence produce innovative nanostructurated tools.
Figure 2 Diphenylalanine based aggregates can be applied with different biotechnological scopes, producing drug delivery systems, hydrogels matrices, supramolecular contrast agents, and fluorescent aggregates. Chemical and functional decorations (like sequences modification, incorporation of fluorescent dyes and conjugation with chelating agents and polymers) at N- and C-terminus of the primary sequence produce innovative nanostructurated tools.CC BY · PubMed Central
Figure 3 Schematic representation of two approaches used for the synthesis of peptide containing liposomes. In route I (pre-liposomal functionalization) a PA is inserted directly during the liposome formulation. In route II (post-liposomal functionalization) a peptide is anchored on the exteral surfaces after liposome formulation by a selective reaction between two functional groups displayed on the peptide and on the liposome, respectively.
Figure 3 Schematic representation of two approaches used for the synthesis of peptide containing liposomes. In route I (pre-liposomal functionalization) a PA is inserted directly during the liposome formulation. In route II (post-liposomal functionalization) a peptide is anchored on the exteral surfaces after liposome formulation by a selective reaction between two functional groups displayed on the peptide and on the liposome, respectively.CC BY · PubMed Central
Figure 4 Structure of targeting peptide sequences: (a) c(RGDfK); (b) Otreotide[c(2–7)-FCFWKTCTol]; (c) [7–14]-Bombesin (H-QWAVGHLM-NH2), and (d) CCK8(H-DYMGWMDF-NH2).
Figure 4 Structure of targeting peptide sequences: (a) c(RGDfK); (b) Otreotide[c(2–7)-FCFWKTCTol]; (c) [7–14]-Bombesin (H-QWAVGHLM-NH2), and (d) CCK8(H-DYMGWMDF-NH2).CC BY · PubMed Central

Verification

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Citations

Cites

No references could be resolved yet.

Research works printed but not linked: 158

  1. Stephanopoulos, 2015, The Powerful Functions of Peptide-Based Bioactive Matrices for Regenerative Medicine, Ann. Biomed. Eng., 43, 501, 10.1007/s10439-014-1166-6 · DOI
  2. Sahoo, 2003, Nanotech approaches to drug delivery and imaging, Drug Discov. Today, 8, 1112, 10.1016/S1359-6446(03)02903-9 · DOI
  3. Panda, 2014, Short peptide based self-assembled nanostructures: Implications in drug delivery and tissue engineering, Polym. Chem., 5, 4418, 10.1039/C4PY00173G · DOI
  4. Brack, 1975, ß structures of alternating polypeptides and their possible prebiotic significance, Nature, 256, 383, 10.1038/256383a0 · DOI
  5. Potekhin, 2001, De novo design of fibrils made of short α-helical coiled coil peptides, Chem. Biol., 8, 1025, 10.1016/S1074-5521(01)00073-4 · DOI
  6. Wagner, 2005, Toward the development of peptide nanofilaments and nanopores as smart materials, Proc. Nat. Acad. Sci. USA, 102, 12656, 10.1073/pnas.0505871102 · DOI
  7. Moutevelis, 2009, A Periodic Table of Coiled-Coil Protein Structures, J. Mol. Biol., 385, 726, 10.1016/j.jmb.2008.11.028 · DOI
  8. Aggeli, 2001, Hierarchical self-assembly of chiral rod-like molecules as a model for peptide β-sheet tapes, ribbons, fibrils, and fibers, Proc. Nat. Acad. Sci. USA, 98, 11857, 10.1073/pnas.191250198 · DOI
  9. Fishwick, 2003, Structures of helical β-tapes and twisted ribbons: The role of side-chain interactions on twist and bend behavior, Nano Lett., 3, 1475, 10.1021/nl034095p · DOI
  10. Aggeli, 2003, pH as a trigger of peptide β-sheet self-assembly and reversible switching between nematic and isotropic phases, J. Am. Chem. Soc., 125, 9619, 10.1021/ja021047i · DOI
  11. Schneider, 2002, Responsive hydrogels from the intramolecular folding and self-assembly of a designed peptide, J. Am. Chem. Soc., 124, 15030, 10.1021/ja027993g · DOI
  12. Veiga, 2012, Arginine-rich self-assembling peptides as potent antibacterial gels, Biomaterials, 33, 8907, 10.1016/j.biomaterials.2012.08.046 · DOI
  13. Reches, 2003, Casting metal nanowires within discrete self-assembled peptide nanotubes, Science, 300, 625, 10.1126/science.1082387 · DOI
  14. 2006, The structure of nanotubes formed by diphenylalanine, the core recognition motif of Alzheimer’s β-amyloid polypeptide, Chem. Comm., 22, 2332
  15. Tamamis, 2009, Self-Assembly of Phenylalanine Oligopeptides: Insights from Experiments and Simulations, Biophys. J., 96, 5020, 10.1016/j.bpj.2009.03.026 · DOI
  16. Yan, 2010, Self-assembly and application of diphenylalanine-based nanostructures, Chem. Soc. Rev., 39, 1877, 10.1039/b915765b · DOI
  17. Kol, 2010, Self-assembled organic nanostructures with metallic-like stiffness, Angew. Chem. Int. Ed., 49, 9939, 10.1002/anie.201002037 · DOI
  18. Wang, 2011, Charged Diphenylalanine Nanotubes and Controlled Hierarchical Self-Assembly, ACS Nano, 5, 4448, 10.1021/nn2016524 · DOI
  19. Vasilev, 2016, Piezoelectric properties of diphenylalaninemicrotubes prepared from the solution, J. Phys. Chem. Solids, 93, 68, 10.1016/j.jpcs.2016.02.002 · DOI
  20. Nikitin, 2016, Low-temperature photoluminescence in self-assembled diphenylalanine microtubes, Phys. Lett. A, 380, 1658, 10.1016/j.physleta.2016.02.043 · DOI
  21. Handelman, 2016, Reconstructive Phase Transition in Ultrashort Peptide Nanostructures and Induced Visible Photoluminescence, Langmuir, 32, 2847, 10.1021/acs.langmuir.5b02784 · DOI
  22. Handelman, 2016, Linear and nonlinear optical waveguiding in bio-inspired peptide nanotubes, Acta Biomater., 30, 72, 10.1016/j.actbio.2015.11.004 · DOI
  23. Reches, 2006, Thermal and chemical stability of diphenylalanine peptide nanotubes: Implications for nanotechnological applications, Langmuir, 22, 1313, 10.1021/la052409d · DOI
  24. Marchesan, 2015, The Phe-Phe motif for peptide self-assembly in nanomedicine, Molecules, 20, 19775, 10.3390/molecules201119658 · DOI
  25. Aronov, 2009, Self-assembled arrays of peptide nanotubes by vapour deposition, Nat. Nanotechnol., 4, 849, 10.1038/nnano.2009.298 · DOI
  26. Scanlon, 2008, Self-assembling peptide nanotubes, Nano Today, 3, 22, 10.1016/S1748-0132(08)70041-0 · DOI
  27. Hendler, 2007, Formation of well-organized self-assembled films from peptide nanotubes, Adv. Mater., 19, 1485, 10.1002/adma.200602265 · DOI
  28. Silva, 2013, l-Diphenylalanine Microtubes As a Potential Drug-Delivery System: Characterization, Release Kinetics, and Cytotoxicity, Langmuir, 29, 10205, 10.1021/la4019162 · DOI
  29. Bonetti, 2015, Dipeptide Nanotubes Containing Unnatural Fluorine-Substituted-Diarylamino Acid and L-Alanine as Candidates for Biomedical Applications, Org. Lett., 17, 4468, 10.1021/acs.orglett.5b02132 · DOI
  30. Emtiazi, 2017, Covalent diphenylalanine peptide nanotube conjugated to folic acid/magnetic nanoparticles for anti-cancer drug delivery, J. Drug Deliv. Sci. Technol., 41, 90, 10.1016/j.jddst.2017.06.005 · DOI
  31. Liu, 2014, Self-Assembling Peptide of D-Amino Acids Boosts Selectivity and Antitumor Efficacy of 10-Hydroxycamptothecin, ACS Appl. Mater. Interfaces, 6, 5558, 10.1021/am406007g · DOI
  32. Li, 2013, Dephosphorylation of D-Peptide Derivatives to Form Biofunctional, Supramolecular Nanofibers/Hydrogels and Their Potential Applications for Intracellular Imaging and Intratumoral Chemotherapy, J. Am. Chem. Soc., 135, 9907, 10.1021/ja404215g · DOI
  33. Zhang, 2015, Enzyme-responsive release of doxorubicin from monodisperse dipeptide-based nanocarriers for highly efficient cancer treatment in vitro, Adv. Funct. Mater., 25, 1193, 10.1002/adfm.201403119 · DOI
  34. Das, 2015, Sticky tubes and magnetic hydrogels co-assembled by a short peptide and melanin-like nanoparticles, Chem. Commun., 51, 5432, 10.1039/C4CC07671K · DOI
  35. Liberato, 2016, Polycaprolactone fibers with self-assembled peptide micro/nanotubes: A practical route towards enhanced mechanical strength and drug delivery applications, J. Mater. Chem. B, 4, 1405, 10.1039/C5TB02240A · DOI
  36. Li, 2016, One-Pot Synthesis of Diphenylalanine-Based Hybrid Nanospheres for Controllable pH- and GSH-Responsive Delivery of Drugs, Chem. Mater., 28, 6584, 10.1021/acs.chemmater.6b02604 · DOI
  37. Jayawarna, 2006, Nanostructured Hydrogels for Three-Dimensional Cell Culture Through Self-Assembly of Fluorenylmethoxycarbonyl-Dipeptides, Adv. Mater., 18, 611, 10.1002/adma.200501522 · DOI
  38. Mao, 2012, Conjugation of two complementary anti-cancer drugs confers molecular hydrogels as a co-delivery system, Chem. Commun., 48, 395, 10.1039/C1CC16250K · DOI
  39. Li, 2013, D-amino acids boost the selectivity and confer supramolecular hydrogels of a nonsteroidal anti-inflammatory drug (NSAID), J. Am. Chem. Soc., 135, 542, 10.1021/ja310019x · DOI
  40. Liang, 2009, Supramolecular Hydrogel of a D-Amino Acid Dipeptide for Controlled Drug Release in Vivo, Langmuir, 25, 8419, 10.1021/la804271d · DOI
  41. Erdogan, 2016, Fabrication of Plasmonic Nanorod-Embedded Dipeptide Microspheres via the Freeze-Quenching Method for Near-Infrared Laser-Triggered Drug-Delivery Applications, Biomacromolecules, 17, 1788, 10.1021/acs.biomac.6b00214 · DOI
  42. Xie, 2016, Calcium-Ion-Triggered Co-assembly of Peptide and Polysaccharide into a Hybrid Hydrogel for Drug Delivery, Nanoscale Res. Lett., 11, 184, 10.1186/s11671-016-1415-8 · DOI
  43. Aviv, M., Halperin-Sternfeld, M., Grigoriants, I., Buzhansky, L., Mironi-Harpaz, I., Seliktar, D., Einav, S., Nevo, Z., and Adler-Abramovich, L. (2018). Improving the Mechanical Rigidity of Hyaluronic Acid by Integration of a Supramolecular Peptide Matrix. ACS Appl. Mater. Interfaces, in press. · DOI
  44. Abbas, 2018, Antitumor Photodynamic Therapy Based on Dipeptide Fibrous Hydrogels with Incorporation of Photosensitive Drugs, ACS Biomater. Sci. Eng., 4, 2046, 10.1021/acsbiomaterials.7b00624 · DOI
  45. Roth-Konforti, M.E., Comune, M., Halperin-Sternfeld, M., Grigoriants, I., Shabat, D., and Adler-Abramovich, L. (2018). UV Light-Responsive Peptide-Based Supramolecular Hydrogel for Controlled Drug Delivery. Macromol. Rapid Commun., in press. · DOI
  46. Diaferia, 2018, Amyloid-Like Fibrillary Morphology Originated by Tyrosine-Containing Aromatic Hexapeptides, Chem. Eur. J., 24, 6804, 10.1002/chem.201800351 · DOI
  47. Diaferia, 2018, Structural Characterization of Self-Assembled Tetra-Tryptophan Based Nanostructures: Variations on a Common Theme, Chem. Phys. Chem., 19, 1635, 10.1002/cphc.201800026 · DOI
  48. Diaferia, 2015, Peptide Materials Obtained by Aggregation of Polyphenylalanine Conjugates as Gadolinium-Based Magnetic Resonance Imaging Contrast Agents, Adv. Funct. Mater., 25, 7003, 10.1002/adfm.201502458 · DOI
  49. Accardo, 2009, Supramolecular aggregates containing lipophilic Gd(III) complexes as contrast agents in MRI, Coord. Chem. Rev., 253, 2193, 10.1016/j.ccr.2009.01.015 · DOI
  50. Diaferia, 2017, Gadolinium containing telechelic PEG-polymers end-capped by di-phenylalanine motives as potential supramolecular MRI contrast agents, J. Pept. Sci., 23, 122, 10.1002/psc.2942 · DOI
  51. Diaferia, 2017, Cross-beta nanostructures based on dinaphthylalanine Gd-conjugates loaded with doxorubicin, Sci. Rep., 7, 307, 10.1038/s41598-017-00332-3 · DOI
  52. Handelman, 2014, Structural and optical properties of short peptides: Nanotubes-to-nanofibers phase transformation, J. Pept. Sci., 20, 487, 10.1002/psc.2661 · DOI
  53. Pinotsi, 2013, A label-free, quantitative assay of amyloid fibril growth based on intrinsic fluorescence, ChemBioChem, 14, 846, 10.1002/cbic.201300103 · DOI
  54. Diaferia, 2016, Hierarchical analysis of self-assembled PEGylated hexaphenylalanine photoluminescent nanostructures, Chem. Eur. J., 22, 16586, 10.1002/chem.201604107 · DOI
  55. Diaferia, 2017, Structural Characterization of PEGylated Hexaphenylalanine Nanostructures Exhibiting Green Photoluminescence Emission, Chem. Eur. J., 23, 14039, 10.1002/chem.201703055 · DOI
  56. Diaferia, 2017, Photoluminescent Peptide-Based Nanostructures as FRET Donor for Fluorophore Dye, Chem. Eur. J., 23, 8741, 10.1002/chem.201701381 · DOI
  57. Morosetti, 1974, Conformational Analysis of Regular Enantiomeric Sequences, Macromolecules, 7, 52, 10.1021/ma60037a011 · DOI
  58. Ghadiri, 1993, Self-assembling organic nanotubes based on a cyclic peptide architecture, Nature, 366, 324, 10.1038/366324a0 · DOI
  59. Chapman, 2012, Design and properties of functional nanotubes from the self-assembly of cyclic peptide templates, Chem. Soc. Rev., 41, 6023, 10.1039/c2cs35172b · DOI
  60. Kim, 2001, Antibacterial agents based on the cyclic d,l-α-peptide architecture, Nature, 412, 452, 10.1038/35086601 · DOI
  61. Ishihara, 2010, Nanofiber formation of amphiphilic cyclic tri-β-peptide, J. Pept. Sci., 16, 110, 10.1002/psc.1206 · DOI
  62. Hartgerink, 1996, Peptide-amphiphile nanofibers: A versatile scaffold for the preparation of self-assembling materials, J. Am. Chem Soc., 118, 43, 10.1021/ja953070s · DOI
  63. Wang, 2014, Doxorubicin-loaded cyclic peptide nanotube bundles overcome chemoresistance in breast cancer cells, J. Biomed. Nanotechnol., 10, 445, 10.1166/jbn.2014.1724 · DOI
  64. Hamley, 2011, Self-assembly of amphiphilic peptides, Soft Matter., 7, 4122, 10.1039/c0sm01218a · DOI
  65. Versluis, 2010, Power struggles in peptide-amphiphile nanostructures, Chem. Soc. Rev., 39, 3434, 10.1039/b919446k · DOI
  66. Vauthey, 2002, Molecular self-assembly of surfactant-like peptides to form nanotubes and nanovesicles, Proc. Natl. Acad. Sci. USA, 99, 5355, 10.1073/pnas.072089599 · DOI
  67. Santoso, 2002, Self-assembly of surfactant-like peptides with variable glycine tails to form nanotubes and nanovesicles, Nano Lett., 2, 687, 10.1021/nl025563i · DOI
  68. Vauthey, 2003, Positively charged surfactant like peptides self-assemble into nanostructures, Langmuir, 19, 4332, 10.1021/la026526+ · DOI
  69. Dehsorkhi, 2013, Interaction between a cationic surfactant-like peptide and lipid vesicles and its relationship to antimicrobial activity, Langmuir, 29, 14246, 10.1021/la403447u · DOI
  70. Holmes, 1993, Spontaneous assembly of a self complementaryoligopeptide to form stable microscopic membrane, Proc. Natl. Acad. Sci. USA, 90, 3334, 10.1073/pnas.90.8.3334 · DOI
  71. Liu, 2012, Molecular binding self assembling peptide EAK16-II with anticancer agent EPT and its implication in cancer cell inhibition, J. Control. Release, 160, 33, 10.1016/j.jconrel.2012.03.009 · DOI
  72. Boettcher, 2001, Comparative cryo-electron microscopy of noncovalent N-dodecanoyl-(d- and l-) serine assemblies in vitreous toluene and water, Langmuir, 17, 873, 10.1021/la001054p · DOI
  73. Fuhrhop, 1993, Molecular monolayer rods and tubules made of .alpha.-(L-lysine),.omega.-(amino) bolaamphiphiles, J. Am. Chem. Soc., 115, 1600, 10.1021/ja00057a069 · DOI
  74. Hartgerink, 2002, Peptide-amphiphilenanofibers: A versatile scaffold for the preparation of self- assembling materials, Proc. Natl. Acad. Sci. USA, 99, 5133, 10.1073/pnas.072699999 · DOI
  75. Matson, 2012, Nanostructure-templated control of drug release from peptide amphiphile nanofiber gels, Soft Matter, 8, 3586, 10.1039/c2sm07420f · DOI
  76. Cui, 2018, Self-Assembly of Giant Peptide, Nanobelts, 16, 9
  77. Yao, 2016, Reducible self-assembling cationic polypeptide-based micelles mediate co-delivery of doxorubicin and microRNA-34a for androgen- independent prostate cancer therapy, J. Control. Release, 232, 203, 10.1016/j.jconrel.2016.04.034 · DOI
  78. Tang, Q., Cao, B., Wu, H., and Cheng, G. (2013). Cholesterol-Peptide Hybrids to Form Liposome-Like Vesicles for Gene Delivery. PLoS ONE. · DOI
  79. Missirlis, 2010, Subsequent Endosomal Disruption Results in SJSA-1, Mol Pharm., 7, 2173, 10.1021/mp100193h · DOI
  80. Pujals, 2006, Mechanistic aspects of cell-penetrating peptide-mediated intracellular drug delivery: Relevance of CPP self-assembly, Biochim. Biophys. Acta Biomembr., 1758, 264, 10.1016/j.bbamem.2006.01.006 · DOI
  81. Agrawal, 2016, CPPsite 2.0: Arepository of experimentally validated cell-penetrating peptides, Nucleic Acids Res., 44, D1098, 10.1093/nar/gkv1266 · DOI
  82. Borrelli, A., Tornesello, A.L., Tornesello, M.L., and Buonaguro, F.M. (2018). Cell Penetrating Peptides as Molecular Carriers for Anti-Cancer Agents. Molecules, 23. · DOI
  83. Sun, 2018, Peptide-decorated polymeric nanomedicines for precision cancer therapy, J. Control. Release, 290, 11, 10.1016/j.jconrel.2018.09.029 · DOI
  84. Gallo, 2019, 1988–2018: Thirty years of drug smuggling at the nano scale. Challenges and opportunities of cell-penetrating peptides in biomedical research, Arch. Biochem. Biophys., 661, 74, 10.1016/j.abb.2018.11.010 · DOI
  85. Zhang, 2013, A pH-responsive α-helical cell penetrating peptide-mediated liposomal delivery system, Biomaterials, 34, 7980, 10.1016/j.biomaterials.2013.07.014 · DOI
  86. Liu, 2014, Legumain protease-activated TAT-liposome cargo for targeting tumours and their microenvironment, Nat. Commun., 5, 4280, 10.1038/ncomms5280 · DOI
  87. Yang, 2014, Preparation and characterization of photo-responsive cell-penetrating peptide-mediated nanostructured lipid carrier, J. Drug Target., 22, 891, 10.3109/1061186X.2014.940589 · DOI
  88. Reubi, 2003, Peptide receptors as molecular targets for cancer diagnosis and therapy, Endocr. Rev., 24, 389, 10.1210/er.2002-0007 · DOI
  89. Accardo, 2014, Influence of PEG length on conformational and binding properties of CCK peptides exposed by supramolecular aggregates, Pept. Sci., 102, 304, 10.1002/bip.22500 · DOI
  90. Ginj, 2006, Radiolabeled somatostatin receptor antagonists are preferable to agonists for in vivo peptide receptor targeting of tumors, Proc. Natl. Acad. Sci. USA, 103, 16436, 10.1073/pnas.0607761103 · DOI
  91. Chan, 2011, Potential mechanisms of prospective antimigraine drugs: A focus on vascular (side) effects, Pharmacol. Ther., 129, 332, 10.1016/j.pharmthera.2010.12.001 · DOI
  92. Codding, P.W. (1998). Conformational analysis from crystallographic data. Structure Based Drug Design, Kluwer Academic. · DOI
  93. Pande, 2010, Phage display: Concept, innovations, applications and future, Biotechnol. Adv., 28, 849, 10.1016/j.biotechadv.2010.07.004 · DOI · Paper page
  94. Ringhieri, 2017, Liposomes derivatized with multimeric copies of KCCYSL peptide as targeting agents for HER-2-overexpressing tumor cells, Int. J. Nanomed., 12, 501, 10.2147/IJN.S113607 · DOI
  95. Ringhieri, 2015, Liposomal doxorubicin doubly functionalized with CCK8 and R8 peptide sequences for selective intracellular drug delivery, J. Pept. Sci., 21, 415, 10.1002/psc.2759 · DOI
  96. Accardo, 2013, Liposomes derivatized with tetrabranchedneurotensin peptides via click chemistry reactions, New J. Chem., 37, 3528, 10.1039/c3nj00596h · DOI
  97. Accardo, 2015, Review peptide-targeted liposomes for selective drug delivery: Advantages and problematic issues, Pept. Sci., 104, 462, 10.1002/bip.22678 · DOI
  98. Feldborg, 2012, Quantitative evaluation of bioorthogonal chemistries for surface functionalization of nanoparticles, Bioconjug. Chem., 23, 2444, 10.1021/bc3005057 · DOI
  99. Wang, 2010, Targeted Polymeric Micelle System for Delivery of Combretastatin A4 to Tumor Vasculature In Vitro, Pharm. Res., 27, 1861, 10.1007/s11095-010-0184-9 · DOI
  100. Miura, 2013, Cyclic RGD-linked polymeric micelles for targeted delivery of platinum anticancer drugs to glioblastoma through the blood-brain tumor barrier, ACS Nano, 7, 8583, 10.1021/nn402662d · DOI
  101. Chen, 2012, Cyclic RGD peptide-modified liposomal drug delivery system: Enhanced cellular uptake in vitro and improved pharmacokinetics in rats, Int. J. Nanomed., 7, 3803, 10.2147/IJN.S33541 · DOI
  102. Amin, 2013, Improvement of pharmacokinetic and antitumor activity of PEGylated liposomal doxorubicin by targeting with N-methylated cyclic RGD peptide in mice bearing C-26 colon carcinomas, Int. J. Pharm., 458, 324, 10.1016/j.ijpharm.2013.10.018 · DOI
  103. Wang, 2014, RGD peptide conjugated liposomal drug delivery system for enhance therapeutic efficacy in treating bone metastasis from prostate cancer, J. Control. Release, 196, 222, 10.1016/j.jconrel.2014.10.012 · DOI
  104. Battistini, 2014, Enhancement of the uptake and cytotoxicactivity of doxorubicin in cancercells by novel cRGD-semipeptide-anchoring liposomes, Mol. Pharm., 11, 2280, 10.1021/mp400718j · DOI
  105. Zhang, 2016, RGD decorated lipid-polymer hybrid nanoparticles for targeted co-delivery of doxorubicin and sorafenib to enhance anti-hepatocellular carcinoma efficacy, Nanomed. Nanotechnol. Biol. Med., 12, 1303, 10.1016/j.nano.2016.01.017 · DOI
  106. Morisco, 2009, Micelles derivatized with octreotide as potential target-selective contrast agents in MRI, J. Pept. Sci., 15, 242, 10.1002/psc.1087 · DOI
  107. Accardo, 2011, Naposomes: A new class of peptide-derivatized, target-selective multimodal nanoparticles for imaging and therapeutic applications, Ther. Deliv., 2, 235, 10.4155/tde.10.86 · DOI
  108. Accardo, 2013, Octreotide labeled aggregates containing platinum complexes as nanovectors for drug delivery, J. Peptsci., 19, 190
  109. Zhang, 2012, The eradication of breast cancer and cancer stem cells using octreotide modified paclitaxel active targeting micelles and salinomycin passive targeting micelles, Biomaterials, 33, 679, 10.1016/j.biomaterials.2011.09.072 · DOI
  110. Zou, 2013, In vivo studies of octreotidemodified N-octyl-O, N-carboxymethyl chitosan micelles loaded with doxorubicin for tumor-targeted delivery, J. Pharm. Sci., 102, 126, 10.1002/jps.23341 · DOI
  111. Xu, 2016, Thailandepsin A-loaded and octreotide-functionalized unimolecular micelles for targeted neuroendocrine cancer therapy, Biomaterials, 91, 1, 10.1016/j.biomaterials.2016.03.010 · DOI
  112. Helbok, 2012, Targeting properties of peptide-modified radiolabeled liposomal nanoparticles, Nanomedicine, 8, 112, 10.1016/j.nano.2011.04.012 · DOI
  113. Li, 2016, Effect of ligand density and PEG modification on octreotide-targetedliposome via somatostatin receptor in vitro and in vivo, Drug Deliv., 23, 3562, 10.1080/10717544.2016.1209797 · DOI
  114. Petersen, 2012, Positron emission tomography evaluation of somatostatin receptor targeted 64Cu-TATE-liposomes in a human neuroendocrine carcinoma mouse model, J. Control. Release, 160, 254, 10.1016/j.jconrel.2011.12.038 · DOI
  115. Chen, 2016, KE108-conjugated unimolecular micelles loaded with a novel HDAC inhibitor thailandepsin-A for targeted neuroendocrine cancer therapy, Biomaterials, 97, 22, 10.1016/j.biomaterials.2016.04.029 · DOI
  116. Chen, 2017, AB3-loaded and tumor-targeted unimolecular micelles for medullary thyroid cancer treatment, J. Mater. Chem. B, 5, 151, 10.1039/C6TB02530G · DOI
  117. Accardo, 2010, Peptide modified nanocarriers for selective targeting of bombesin receptors, Mol. Biosyst., 6, 878, 10.1039/b923147a · DOI
  118. Accardo, 2012, Peptide-modified liposomes for selective targeting of bombesin receptors overexpressed by cancer cells: A potential theranostic agent, Int. J. Nanomed., 7, 2007
  119. Ringhieri, 2014, Target selective micelles for bombesin receptors incorporating Au(III)-dithiocarbamato complexes, Int. J. Pharmaceut., 473, 194, 10.1016/j.ijpharm.2014.07.014 · DOI
  120. Accardo, 2013, Bombesin peptide antagonist for target-selective delivery of liposomal doxorubicin on cancer cells, J. Drug Target., 21, 240, 10.3109/1061186X.2012.741138 · DOI
  121. Accardo, 2007, High-relaxivity supramolecular aggregates containing peptide and Gd complexes agents in MRI, J. Biol. Inorg. Chem., 12, 267, 10.1007/s00775-006-0186-6 · DOI
  122. Gasparini, 1998, Vascular integrin αvβ3: A new prognostic indicator in breast cancer, Clin. Cancer Res., 4, 2625
  123. Liu, 2006, Radiolabeled multimeric cyclic RGD peptides as integrin alphavbeta3 targeted radiotracers for tumor imaging, Mol. Pharm., 3, 472, 10.1021/mp060049x · DOI
  124. Xiong, 2005, Enhanced intracellular delivery and improved antitumor efficacy of doxorubicin by sterically stabilized liposomes modified with a synthetic RGD mimetic, J. Control. Release, 107, 262, 10.1016/j.jconrel.2005.03.030 · DOI
  125. Danhier, 2012, RGD-based strategies to target alpha(v) beta(3) integrin in cancer therapy and diagnosis, Mol. Pharm., 9, 2961, 10.1021/mp3002733 · DOI
  126. Schiffelers, R.M., Koning, G.A., ten Hagen, T.L.M., Fens, M.H.A.M., Schraa, A.J., Janssen, A.P.C.A., Kok, R.J., Molema, G., and Storm, G. (2003). Anti-tumor efficacy of tumor vasculature-targeted liposomal doxorubicin. J. Control. Release, 115–122. · DOI
  127. Murphy, 2008, Nanoparticle-mediated drug delivery to tumor vasculature suppresses metastasis, Proc Natl. Acad. Sci. USA, 105, 9343, 10.1073/pnas.0803728105 · DOI
  128. Guan, 2016, Cyclic RGD targeting cisplatin micelles for near-infrared imaging-guided chemotherapy, RSC Advances, 6, 1151, 10.1039/C5RA19711B · DOI
  129. Zhao, 2009, RGD-based strategies for improving antitumor activity of paclitaxel-loaded liposomes in nude mice xenografted with human ovarian cancer, J. Drug Target., 17, 10, 10.1080/10611860802368966 · DOI
  130. Meng, 2010, Enhanced antitumor effect of novel dual-targeted paclitaxel liposomes, Nanotechnology, 21, 415103, 10.1088/0957-4484/21/41/415103 · DOI
  131. Li, 2014, RGD-fatty alcohol-modified docetaxel liposomes improve tumor selectivity in vivo, Int. J. Pharm., 468, 133, 10.1016/j.ijpharm.2014.04.001 · DOI
  132. Pattillo, 2005, Targeting of the antivascular drug combretastatin to irradiated tumors results in tumor growth delay, Pharm. Res., 22, 1117, 10.1007/s11095-005-5646-0 · DOI
  133. Dubey, 2004, Liposomes modified with cyclic RGD peptide for tumor targeting, J. Drug Target., 12, 257, 10.1080/10611860410001728040 · DOI
  134. Garg, 2009, Targeting colon cancer cells using PEGylated liposomes modified with a fibronectin-mimetic peptide, Int. J. Pharm., 366, 201, 10.1016/j.ijpharm.2008.09.016 · DOI
  135. Kessler, 1986, Peptidkonformationen, 39. NMR-studien zur konformation von cyclopentapeptidanalogen des thymopoietins, Liebigs Ann. Chem., 1986, 893, 10.1002/jlac.198619860508 · DOI
  136. Kessler, 1995, Design of superactive and selective integrin receptor antagonists containing the RGD sequence, Lett. Pep. Sci., 2, 155, 10.1007/BF00119142 · DOI
  137. Haubner, 1996, Structural and functional aspects of RGD-containing cyclic pentapeptides as highly potent and selective integrin v 3 antagonists, J. Am. Chem. Soc., 118, 7461, 10.1021/ja9603721 · DOI
  138. Wang, 2009, RGD-modified polymeric micelles as potential carriers for targeted delivery to integrin-overexpressing tumor vasculature and tumor cells, J. Drug Target., 17, 459, 10.1080/10611860902974085 · DOI
  139. Kazuki, 2009, Tissue-Penetrating Delivery of Compounds and Nanoparticles into Tumors, Cancer Cell, 6, 510
  140. Gao, 2017, iRGD-modified lipid–polymer hybrid nanoparticles loaded with isoliquiritigenin to enhance anti-breast cancer effect and tumor-targeting ability, Int. J. Nanomed., 12, 4147, 10.2147/IJN.S134148 · DOI
  141. Jiang, 2018, Design of an AmphiphilicRGD Peptide and Self-Assembling Nanovesicles for Improving Tumor Accumulation and Penetration and the Photodynamic Efficacy of the Photosensitizer, ACS Appl. Mater. Interfaces, 10, 31674, 10.1021/acsami.8b11699 · DOI
  142. Hu, 2018, iRGD-decorated reduction-responsive nanoclusters for targeted drug delivery, Nanoscale, 10, 10514, 10.1039/C8NR02534G · DOI
  143. Melacini, 1997, Multiconformational NMR Analysis of Sandostatin (Octreotide): Equilibrium between beta-Sheet and Partially Helical Structures, Biochemistry, 36, 1233, 10.1021/bi962497o · DOI
  144. Cuttitta, 1985, Bombesin-like peptides can function as autocrine growth factors in human small-cell lung cancer, Nature, 16, 823, 10.1038/316823a0 · DOI
  145. Patel, 2006, Gastrin-releasing peptide and cancer, Biochim. Biophys. Acta, 1766, 23
  146. Smith, 2005, Radiolabeled peptide conjugates for targeting of the bombesin receptor superfamily subtypes, Nucl. Med. Biol., 32, 733, 10.1016/j.nucmedbio.2005.05.005 · DOI
  147. Parry, 2007, In vitro and in vivo evaluation of 64Cu-labeled DOTA-linker-bombesin(7–14) analogues containing different amino acid linker moieties, Bioconjug. Chem., 18, 1110, 10.1021/bc0603788 · DOI
  148. Jamous, 2014, RPEG spacers of different length influence the biological profile of bombesin-based radiolabeled antagonists, Nucl. Med. Biol., 41, 464, 10.1016/j.nucmedbio.2014.03.014 · DOI
  149. Bernhard, 2016, Direct subphthalocyanine conjugation to bombesin vs. indirect conjugation to its lipidic nanocarrier, Org. Biomol. Chem., 14, 4511, 10.1039/C6OB00530F · DOI
  150. Pellegrini, 1999, Molecular complex of cholecystokinin-8 and N-terminus of the cholecystokinin A receptor by NMR spectroscopy, Biochemistry, 38, 14775, 10.1021/bi991272l · DOI
  151. Morelli, 2002, CCK8 peptide derivatized with diphenylphosphine for rhenium labelling: Synthesis and molecular mechanics calculations, Pept. Sci., 8, 373, 10.1002/psc.400 · DOI
  152. Accardo, 2011, Amphiphilic CCK peptides assembled in supramolecular aggregates: Structural investigations and in vitro studies, Mol. Biosyst., 7, 862, 10.1039/C0MB00238K · DOI
  153. Tesauro, 2007, Peptide derivatizedlamellar aggregates as target-specific MRI contrast agents, Chembiochem, 8, 950, 10.1002/cbic.200700077 · DOI
  154. Accardo, 2008, Peptide-containing aggregates as selective nanocarriers for therapeutics, Chem. Med. Chem., 3, 594, 10.1002/cmdc.200700269 · DOI
  155. Vincenzi, 2015, Intrinsically disordered amphiphilic peptides as potential targets in drug delivery vehicles, Mol. Biosyst., 11, 2925, 10.1039/C5MB00358J · DOI
  156. Accardo, 2013, Solution conformational features and interfacial properties of an intrinsically disordered peptide coupled to alkyl chains: A new class of peptide amphiphiles, Mol. Biosyst., 9, 1401, 10.1039/c3mb25507g · DOI
  157. Vincenzi, 2015, Conformational ensembles explored dynamically from disordered peptides targeting chemokine receptor CXCR4, Int. J. Mol. Sci., 16, 12159, 10.3390/ijms160612159 · DOI
  158. Banta, 2007, Engineering protein and peptide building blocks for nanotechnology, J. Nanosci. Nanotechnol., 7, 387, 10.1166/jnn.2007.153 · DOI

Cited by

Sorted by citations

Metadata

Authors
Tesauro, D., Accardo, A., Diaferia, C., Milano, V., Guillon, J., Ronga, L., & Rossi, F.
Venue
Molecules
Publisher
MDPI AG
Published
2019-01-19
Volume
24
Issue
2
Pages
351
ISSN
1420-3049
DOI
10.3390/molecules24020351
PMC
PMC6359574
Cited by
225
References
0
Language
en
Licence
creativecommons.org/licenses/by/4.0/ (vor)

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review