Bombesin peptide antagonist for target-selective delivery of liposomal doxorubicin on cancer cells (410 views)
Journal Of Drug Targeting (ISSN: 1061-186x), 2012 Nov 21; 21(3): 240-249.
Export to BibTeX Export to EndNote
Paper type: Journal Article,
Impact factor: 2.768, 5-year impact factor: 2.995
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-84875916349&partnerID=40&md5=ef8abd66c5be566233dee4f5443dc39a
Keywords: Animal Studies, Anticancer Efficacy, Bombesin Peptide, Doxorubicin Delivery, Liposomes For Drug Delivery, Amino Acid Derivative, Amphophile, Bombesin Antagonist, Bombesin Receptor, Indium 111, Lutetium 177, Macrogol, Pentetic Acid, Peptide Derivative, Tetraxetan, Amino Acid Sequence, Animal Experiment, Animal Model, Article, Binding Affinity, Binding Assay, Binding Site, Cancer Cell, Cancer Inhibition, Cell Survival, Cell Viability, Controlled Study, Cytotoxicity, Drug Delivery System, Drug Efficacy, Drug Selectivity, Drug Stability, Drug Targeting, Female, High Performance Liquid Chromatography, Human, Human Tissue, Hydrophobicity, In Vitro Study, In Vivo Study, Incubation Temperature, Isotope Labeling, Mouse, Nonhuman, Peptide Synthesis, Priority Journal, Prostate Cancer, Receptor Affinity, Tumor Growth, Tumor Volume, Tumor Xenograft, Weight Reduction, Zeta Potential,
Affiliations:
*** IBB - CNR ***
CIRPeB, Department of Biological Sciences, University of Naples Federico II, Napoli, Italy
Invectors Srl, Napoli, Italy
Division of Radiological Chemistry, University Hospital Basel, Basel, Switzerland
Department of Pharmaceutical and Toxicological Chemistry, University of Naples Federico II, Napoli, Italy
Department of Nuclear Medicine, Istituto Nazionale per Lo Studio e la Cura Dei Tumori, Fondazione G. Pascale, Napoli, Italy
Department of Experimental Pharmacology, University of Naples Federico II, Napoli, Italy
References:
Abiraj, K., Mansi, R., Tamma, M.L., Fani, M., Forrer, F., Nicolas, G., Cescato, R., Maecke, H.R., Bombesin antagonist-based radioligands for translational nuclear imaging of gastrin-releasing peptide receptor-positive tumors (2011) J Nucl Med, 52, pp. 1970-197
Accardo, A., Tesauro, D., Aloj, L., Tarallo, L., Arra, C., Mangiapia, G., Vaccaro, M., Morelli, G., Peptidecontaining aggregates as selective nanocarriers for therapeutics (2008) ChemMedChem, 3, pp. 594-602
Accardo, A., Mansi, R., Morisco, A., Mangiapia, G., Paduano, L., Tesauro, D., Radulescu, A., Morelli, G., Peptide modified nanocarriers for selective targeting of bombesin receptors (2010) Mol Biosyst, 6, pp. 878-887
Accardo, A., Salsano, G., Morisco, A., Aurilio, M., Parisi, A., Maione, F., Cicala, C., Morelli, G., Peptidemodified liposomes for selective targeting of bombesin receptors overexpressed by cancer cells: A potential theranostic agent (2012) Int J Nanomedicine, 7, pp. 2007-2017
Battey, J.F., Way, J.M., Corjay, M.H., Shapira, H., Kusano, K., Harkins, R., Wu, J.M., Feldman, R.I., Molecular cloning of the bombesin/gastrin-releasing peptide receptor from Swiss 3T3 cells (1991) Proc Natl Acad Sci USA, 88, pp. 395-399
Chan, K.Y., Vermeersch, S., De Hoon, J., Villalón, C.M., Maassenvandenbrink, A., Potential mechanisms of prospective antimigraine drugs: A focus on vascular (side) effects (2011) Pharmacol Ther, 129, pp. 332-351
Chanda, N., Kattumuri, V., Shukla, R., Zambre, A., Katti, K., Upendran, A., Kulkarni, R.R., Kannan, R., Bombesin functionalized gold nanoparticles show in vitro and in vivo cancer receptor specificity (2010) Proc Natl Acad Sci USA, 107, pp. 8760-8765
Chang, W.C., White, P.D., (2000) Fmoc Solid Phase Peptide Synthesis, , Oxford, UK: Oxford Univ Press
Fathi, Z., Corjay, M.H., Shapira, H., Wada, E., Benya, R., Jensen, R., Viallet, J., Battey, J.F., BRS-3: A novel bombesin receptor subtype selectively expressed in testis and lung carcinoma cells (1993) J Biol Chem, 268, pp. 5979-5984
Fleischmann, A., Waser, B., Reubi, J.C., Overexpression of gastrinreleasing peptide receptors in tumor-associated blood vessels of human ovarian neoplasms (2007) Cell Oncol, 29, pp. 421-433
Gugger, M., Reubi, J.C., Gastrin-releasing peptide receptors in non-neoplastic and neoplastic human breast (1999) Am J Pathol, 155, pp. 2067-2076
Höhne, A., Mu, L., Honer, M., Schubiger, P.A., Ametamey, S.M., Graham, K., Stellfeld, T., Srinivasan, A., Synthesis, 18F-labeling, and in vitro and in vivo studies of bombesin peptides modified with silicon-based building blocks (2008) Bioconjug Chem, 19, pp. 1871-1879
Hosta-Rigau, L., Olmedo, I., Arbiol, J., Cruz, L.J., Kogan, M.J., Albericio, F., Multifunctionalized gold nanoparticles with peptides targeted to gastrin-releasing peptide receptor of a tumor cell line (2010) Bioconjug Chem, 21, pp. 1070-1078
Lee, C.M., Jeong, H.J., Cheong, S.J., Kim, E.M., Kim, D.W., Lim, S.T., Sohn, M.H., Prostate cancer-targeted imaging using magnetofluorescent polymeric nanoparticles functionalized with bombesin (2010) Pharm Res, 27, pp. 712-721
Llinares, M., Devin, C., Chaloin, O., Azay, J., Noel-Artis, A.M., Bernad, N., Fehrentz, J.A., Martinez, J., Syntheses and biological activities of potent bombesin receptor antagonists (1999) J Pept Res, 53, pp. 275-283
Mansi, R., Wang, X., Forrer, F., Kneifel, S., Tamma, M.L., Waser, B., Cescato, R., Maecke, H.R., Evaluation of a 1,4,7,10-tetraazacyclododecane-1,4,7,10-tetraacetic acid-conjugated bombesin-based radioantagonist for the labeling with single-photon emission computed tomography, positron emission tomography, and therapeutic radionuclides (2009) Clin Cancer Res, 15, pp. 5240-5249
Markwalder, R., Reubi, J.C., Gastrin-releasing peptide receptors in the human prostate: Relation to neoplastic transformation (1999) Cancer Res, 59, pp. 1152-1159
Martin, A.L., Hickey, J.L., Ablack, A.L., Lewis, J.D., Luyt, L.G., Gillies, E.R., Synthesis of bombesin-functionalized iron oxide nanoparticles and their specific uptake in prostate cancer cells (2009) J Nanopart Res, 12, pp. 1599-1608
Mendoza-Sánchez, A.N., Ferro-Flores, G., Ocampo-García, B.E., Morales-Avila, E., De, M., Ramírez, F., De León-Rodríguez, L.M., Camacho-López, M.A., Lys3-bombesin conjugated to 99mTc-labelled gold nanoparticles for in vivo gastrin releasing peptide-receptor imaging (2010) J Biomed Nanotechnol, 6, pp. 375-384
Nagalla, S.R., Barry, B.J., Creswick, K.C., Eden, P., Taylor, J.T., Spindel, E.R., Cloning of a receptor for amphibian [Phe13]bombesin distinct from the receptor for gastrin-releasing peptide: Identification of a fourth bombesin receptor subtype (BB4) (1995) Proc Natl Acad Sci USA, 92, pp. 6205-6209
Parry, J.J., Kelly, T.S., Andrews, R., Rogers, B.E., In vitro and in vivo evaluation of 64Cu-labeled DOTA-linker-bombesin(7- 14) analogues containing different amino acid linker moieties (2007) Bioconjug Chem, 18, pp. 1110-1117
Rogers, B.E., Bigott, H.M., McCarthy, D.W., Della Manna, D., Kim, J., Sharp, T.L., Welch, M.J., MicroPET imaging of a gastrin-releasing peptide receptor-positive tumor in a mouse model of human prostate cancer using a 64Cu-labeled bombesin analogue (2003) Bioconjug Chem, 14, pp. 756-763
Schmitt, L., Dietrich, C., Synthesis and characterization of chelatorlipids for reversible immobilization of engineered proteins at selfassembled lipid interfaces (2004) J Am Chem Soc, 116, pp. 8485-8491
Smith, C.J., Volkert, W.A., Hoffman, T.J., Radiolabeled peptide conjugates for targeting of the bombesin receptor superfamily subtypes (2005) Nucl Med Biol, 32, pp. 733-740
Stewart, J.C., Colorimetric determination of phospholipids with ammonium ferrothiocyanate (1980) Anal Biochem, 104, pp. 10-14
Wada, E., Way, J., Shapira, H., Kusano, K., Lebacq-Verheyden, A.M., Coy, D., Jensen, R., Battery, J., CDNA cloning, characterization, and brain region-specific expression of a neuromedin-B-preferring bombesin receptor (1991) Neuron, 6, pp. 421-430
Zhu, Y.F., Chen, C., Recent advances in small molecule gonadotrophin-releasing hormone receptor antagonists (2004) Expert Opin Ther Pat, 14, pp. 187-199
Battey, J. F., Way, J. M., Corjay, M. H., Shapira, H., Kusano, K., Harkins, R., Wu, J. M., Feldman, R. I., Molecular cloning of the bombesin/gastrin-releasing peptide receptor from Swiss 3T3 cells (1991) Proc Natl Acad Sci USA, 88, pp. 395-399
Chan, K. Y., Vermeersch, S., De Hoon, J., Villal n, C. M., Maassenvandenbrink, A., Potential mechanisms of prospective antimigraine drugs: A focus on vascular (side) effects (2011) Pharmacol Ther, 129, pp. 332-351
Chang, W. C., White, P. D., (2000) Fmoc Solid Phase Peptide Synthesis, , Oxford, UK: Oxford Univ Press
H hne, A., Mu, L., Honer, M., Schubiger, P. A., Ametamey, S. M., Graham, K., Stellfeld, T., Srinivasan, A., Synthesis, 18F-labeling, and in vitro and in vivo studies of bombesin peptides modified with silicon-based building blocks (2008) Bioconjug Chem, 19, pp. 1871-1879
Lee, C. M., Jeong, H. J., Cheong, S. J., Kim, E. M., Kim, D. W., Lim, S. T., Sohn, M. H., Prostate cancer-targeted imaging using magnetofluorescent polymeric nanoparticles functionalized with bombesin (2010) Pharm Res, 27, pp. 712-721
Martin, A. L., Hickey, J. L., Ablack, A. L., Lewis, J. D., Luyt, L. G., Gillies, E. R., Synthesis of bombesin-functionalized iron oxide nanoparticles and their specific uptake in prostate cancer cells (2009) J Nanopart Res, 12, pp. 1599-1608
Mendoza-S nchez, A. N., Ferro-Flores, G., Ocampo-Garc a, B. E., Morales-Avila, E., De, M., Ram rez, F., De Le n-Rodr guez, L. M., Camacho-L pez, M. A., Lys3-bombesin conjugated to 99mTc-labelled gold nanoparticles for in vivo gastrin releasing peptide-receptor imaging (2010) J Biomed Nanotechnol, 6, pp. 375-384
Nagalla, S. R., Barry, B. J., Creswick, K. C., Eden, P., Taylor, J. T., Spindel, E. R., Cloning of a receptor for amphibian [Phe13] bombesin distinct from the receptor for gastrin-releasing peptide: Identification of a fourth bombesin receptor subtype (BB4) (1995) Proc Natl Acad Sci USA, 92, pp. 6205-6209
Parry, J. J., Kelly, T. S., Andrews, R., Rogers, B. E., In vitro and in vivo evaluation of 64Cu-labeled DOTA-linker-bombesin (7- 14) analogues containing different amino acid linker moieties (2007) Bioconjug Chem, 18, pp. 1110-1117
Rogers, B. E., Bigott, H. M., McCarthy, D. W., Della Manna, D., Kim, J., Sharp, T. L., Welch, M. J., MicroPET imaging of a gastrin-releasing peptide receptor-positive tumor in a mouse model of human prostate cancer using a 64Cu-labeled bombesin analogue (2003) Bioconjug Chem, 14, pp. 756-763
Smith, C. J., Volkert, W. A., Hoffman, T. J., Radiolabeled peptide conjugates for targeting of the bombesin receptor superfamily subtypes (2005) Nucl Med Biol, 32, pp. 733-740
Stewart, J. C., Colorimetric determination of phospholipids with ammonium ferrothiocyanate (1980) Anal Biochem, 104, pp. 10-14
Zhu, Y. F., Chen, C., Recent advances in small molecule gonadotrophin-releasing hormone receptor antagonists (2004) Expert Opin Ther Pat, 14, pp. 187-199
Journal Of Drug Targeting (ISSN: 1061-186x), 2012 Nov 21; 21(3): 240-249.
Export to BibTeX Export to EndNote
Paper type: Journal Article,
Impact factor: 2.768, 5-year impact factor: 2.995
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-84875916349&partnerID=40&md5=ef8abd66c5be566233dee4f5443dc39a
Keywords: Animal Studies, Anticancer Efficacy, Bombesin Peptide, Doxorubicin Delivery, Liposomes For Drug Delivery, Amino Acid Derivative, Amphophile, Bombesin Antagonist, Bombesin Receptor, Indium 111, Lutetium 177, Macrogol, Pentetic Acid, Peptide Derivative, Tetraxetan, Amino Acid Sequence, Animal Experiment, Animal Model, Article, Binding Affinity, Binding Assay, Binding Site, Cancer Cell, Cancer Inhibition, Cell Survival, Cell Viability, Controlled Study, Cytotoxicity, Drug Delivery System, Drug Efficacy, Drug Selectivity, Drug Stability, Drug Targeting, Female, High Performance Liquid Chromatography, Human, Human Tissue, Hydrophobicity, In Vitro Study, In Vivo Study, Incubation Temperature, Isotope Labeling, Mouse, Nonhuman, Peptide Synthesis, Priority Journal, Prostate Cancer, Receptor Affinity, Tumor Growth, Tumor Volume, Tumor Xenograft, Weight Reduction, Zeta Potential,
Affiliations:
*** IBB - CNR ***
CIRPeB, Department of Biological Sciences, University of Naples Federico II, Napoli, Italy
Invectors Srl, Napoli, Italy
Division of Radiological Chemistry, University Hospital Basel, Basel, Switzerland
Department of Pharmaceutical and Toxicological Chemistry, University of Naples Federico II, Napoli, Italy
Department of Nuclear Medicine, Istituto Nazionale per Lo Studio e la Cura Dei Tumori, Fondazione G. Pascale, Napoli, Italy
Department of Experimental Pharmacology, University of Naples Federico II, Napoli, Italy
References:
Abiraj, K., Mansi, R., Tamma, M.L., Fani, M., Forrer, F., Nicolas, G., Cescato, R., Maecke, H.R., Bombesin antagonist-based radioligands for translational nuclear imaging of gastrin-releasing peptide receptor-positive tumors (2011) J Nucl Med, 52, pp. 1970-197
Accardo, A., Tesauro, D., Aloj, L., Tarallo, L., Arra, C., Mangiapia, G., Vaccaro, M., Morelli, G., Peptidecontaining aggregates as selective nanocarriers for therapeutics (2008) ChemMedChem, 3, pp. 594-602
Accardo, A., Mansi, R., Morisco, A., Mangiapia, G., Paduano, L., Tesauro, D., Radulescu, A., Morelli, G., Peptide modified nanocarriers for selective targeting of bombesin receptors (2010) Mol Biosyst, 6, pp. 878-887
Accardo, A., Salsano, G., Morisco, A., Aurilio, M., Parisi, A., Maione, F., Cicala, C., Morelli, G., Peptidemodified liposomes for selective targeting of bombesin receptors overexpressed by cancer cells: A potential theranostic agent (2012) Int J Nanomedicine, 7, pp. 2007-2017
Battey, J.F., Way, J.M., Corjay, M.H., Shapira, H., Kusano, K., Harkins, R., Wu, J.M., Feldman, R.I., Molecular cloning of the bombesin/gastrin-releasing peptide receptor from Swiss 3T3 cells (1991) Proc Natl Acad Sci USA, 88, pp. 395-399
Chan, K.Y., Vermeersch, S., De Hoon, J., Villalón, C.M., Maassenvandenbrink, A., Potential mechanisms of prospective antimigraine drugs: A focus on vascular (side) effects (2011) Pharmacol Ther, 129, pp. 332-351
Chanda, N., Kattumuri, V., Shukla, R., Zambre, A., Katti, K., Upendran, A., Kulkarni, R.R., Kannan, R., Bombesin functionalized gold nanoparticles show in vitro and in vivo cancer receptor specificity (2010) Proc Natl Acad Sci USA, 107, pp. 8760-8765
Chang, W.C., White, P.D., (2000) Fmoc Solid Phase Peptide Synthesis, , Oxford, UK: Oxford Univ Press
Fathi, Z., Corjay, M.H., Shapira, H., Wada, E., Benya, R., Jensen, R., Viallet, J., Battey, J.F., BRS-3: A novel bombesin receptor subtype selectively expressed in testis and lung carcinoma cells (1993) J Biol Chem, 268, pp. 5979-5984
Fleischmann, A., Waser, B., Reubi, J.C., Overexpression of gastrinreleasing peptide receptors in tumor-associated blood vessels of human ovarian neoplasms (2007) Cell Oncol, 29, pp. 421-433
Gugger, M., Reubi, J.C., Gastrin-releasing peptide receptors in non-neoplastic and neoplastic human breast (1999) Am J Pathol, 155, pp. 2067-2076
Höhne, A., Mu, L., Honer, M., Schubiger, P.A., Ametamey, S.M., Graham, K., Stellfeld, T., Srinivasan, A., Synthesis, 18F-labeling, and in vitro and in vivo studies of bombesin peptides modified with silicon-based building blocks (2008) Bioconjug Chem, 19, pp. 1871-1879
Hosta-Rigau, L., Olmedo, I., Arbiol, J., Cruz, L.J., Kogan, M.J., Albericio, F., Multifunctionalized gold nanoparticles with peptides targeted to gastrin-releasing peptide receptor of a tumor cell line (2010) Bioconjug Chem, 21, pp. 1070-1078
Lee, C.M., Jeong, H.J., Cheong, S.J., Kim, E.M., Kim, D.W., Lim, S.T., Sohn, M.H., Prostate cancer-targeted imaging using magnetofluorescent polymeric nanoparticles functionalized with bombesin (2010) Pharm Res, 27, pp. 712-721
Llinares, M., Devin, C., Chaloin, O., Azay, J., Noel-Artis, A.M., Bernad, N., Fehrentz, J.A., Martinez, J., Syntheses and biological activities of potent bombesin receptor antagonists (1999) J Pept Res, 53, pp. 275-283
Mansi, R., Wang, X., Forrer, F., Kneifel, S., Tamma, M.L., Waser, B., Cescato, R., Maecke, H.R., Evaluation of a 1,4,7,10-tetraazacyclododecane-1,4,7,10-tetraacetic acid-conjugated bombesin-based radioantagonist for the labeling with single-photon emission computed tomography, positron emission tomography, and therapeutic radionuclides (2009) Clin Cancer Res, 15, pp. 5240-5249
Markwalder, R., Reubi, J.C., Gastrin-releasing peptide receptors in the human prostate: Relation to neoplastic transformation (1999) Cancer Res, 59, pp. 1152-1159
Martin, A.L., Hickey, J.L., Ablack, A.L., Lewis, J.D., Luyt, L.G., Gillies, E.R., Synthesis of bombesin-functionalized iron oxide nanoparticles and their specific uptake in prostate cancer cells (2009) J Nanopart Res, 12, pp. 1599-1608
Mendoza-Sánchez, A.N., Ferro-Flores, G., Ocampo-García, B.E., Morales-Avila, E., De, M., Ramírez, F., De León-Rodríguez, L.M., Camacho-López, M.A., Lys3-bombesin conjugated to 99mTc-labelled gold nanoparticles for in vivo gastrin releasing peptide-receptor imaging (2010) J Biomed Nanotechnol, 6, pp. 375-384
Nagalla, S.R., Barry, B.J., Creswick, K.C., Eden, P., Taylor, J.T., Spindel, E.R., Cloning of a receptor for amphibian [Phe13]bombesin distinct from the receptor for gastrin-releasing peptide: Identification of a fourth bombesin receptor subtype (BB4) (1995) Proc Natl Acad Sci USA, 92, pp. 6205-6209
Parry, J.J., Kelly, T.S., Andrews, R., Rogers, B.E., In vitro and in vivo evaluation of 64Cu-labeled DOTA-linker-bombesin(7- 14) analogues containing different amino acid linker moieties (2007) Bioconjug Chem, 18, pp. 1110-1117
Rogers, B.E., Bigott, H.M., McCarthy, D.W., Della Manna, D., Kim, J., Sharp, T.L., Welch, M.J., MicroPET imaging of a gastrin-releasing peptide receptor-positive tumor in a mouse model of human prostate cancer using a 64Cu-labeled bombesin analogue (2003) Bioconjug Chem, 14, pp. 756-763
Schmitt, L., Dietrich, C., Synthesis and characterization of chelatorlipids for reversible immobilization of engineered proteins at selfassembled lipid interfaces (2004) J Am Chem Soc, 116, pp. 8485-8491
Smith, C.J., Volkert, W.A., Hoffman, T.J., Radiolabeled peptide conjugates for targeting of the bombesin receptor superfamily subtypes (2005) Nucl Med Biol, 32, pp. 733-740
Stewart, J.C., Colorimetric determination of phospholipids with ammonium ferrothiocyanate (1980) Anal Biochem, 104, pp. 10-14
Wada, E., Way, J., Shapira, H., Kusano, K., Lebacq-Verheyden, A.M., Coy, D., Jensen, R., Battery, J., CDNA cloning, characterization, and brain region-specific expression of a neuromedin-B-preferring bombesin receptor (1991) Neuron, 6, pp. 421-430
Zhu, Y.F., Chen, C., Recent advances in small molecule gonadotrophin-releasing hormone receptor antagonists (2004) Expert Opin Ther Pat, 14, pp. 187-199
Battey, J. F., Way, J. M., Corjay, M. H., Shapira, H., Kusano, K., Harkins, R., Wu, J. M., Feldman, R. I., Molecular cloning of the bombesin/gastrin-releasing peptide receptor from Swiss 3T3 cells (1991) Proc Natl Acad Sci USA, 88, pp. 395-399
Chan, K. Y., Vermeersch, S., De Hoon, J., Villal n, C. M., Maassenvandenbrink, A., Potential mechanisms of prospective antimigraine drugs: A focus on vascular (side) effects (2011) Pharmacol Ther, 129, pp. 332-351
Chang, W. C., White, P. D., (2000) Fmoc Solid Phase Peptide Synthesis, , Oxford, UK: Oxford Univ Press
H hne, A., Mu, L., Honer, M., Schubiger, P. A., Ametamey, S. M., Graham, K., Stellfeld, T., Srinivasan, A., Synthesis, 18F-labeling, and in vitro and in vivo studies of bombesin peptides modified with silicon-based building blocks (2008) Bioconjug Chem, 19, pp. 1871-1879
Lee, C. M., Jeong, H. J., Cheong, S. J., Kim, E. M., Kim, D. W., Lim, S. T., Sohn, M. H., Prostate cancer-targeted imaging using magnetofluorescent polymeric nanoparticles functionalized with bombesin (2010) Pharm Res, 27, pp. 712-721
Martin, A. L., Hickey, J. L., Ablack, A. L., Lewis, J. D., Luyt, L. G., Gillies, E. R., Synthesis of bombesin-functionalized iron oxide nanoparticles and their specific uptake in prostate cancer cells (2009) J Nanopart Res, 12, pp. 1599-1608
Mendoza-S nchez, A. N., Ferro-Flores, G., Ocampo-Garc a, B. E., Morales-Avila, E., De, M., Ram rez, F., De Le n-Rodr guez, L. M., Camacho-L pez, M. A., Lys3-bombesin conjugated to 99mTc-labelled gold nanoparticles for in vivo gastrin releasing peptide-receptor imaging (2010) J Biomed Nanotechnol, 6, pp. 375-384
Nagalla, S. R., Barry, B. J., Creswick, K. C., Eden, P., Taylor, J. T., Spindel, E. R., Cloning of a receptor for amphibian [Phe13] bombesin distinct from the receptor for gastrin-releasing peptide: Identification of a fourth bombesin receptor subtype (BB4) (1995) Proc Natl Acad Sci USA, 92, pp. 6205-6209
Parry, J. J., Kelly, T. S., Andrews, R., Rogers, B. E., In vitro and in vivo evaluation of 64Cu-labeled DOTA-linker-bombesin (7- 14) analogues containing different amino acid linker moieties (2007) Bioconjug Chem, 18, pp. 1110-1117
Rogers, B. E., Bigott, H. M., McCarthy, D. W., Della Manna, D., Kim, J., Sharp, T. L., Welch, M. J., MicroPET imaging of a gastrin-releasing peptide receptor-positive tumor in a mouse model of human prostate cancer using a 64Cu-labeled bombesin analogue (2003) Bioconjug Chem, 14, pp. 756-763
Smith, C. J., Volkert, W. A., Hoffman, T. J., Radiolabeled peptide conjugates for targeting of the bombesin receptor superfamily subtypes (2005) Nucl Med Biol, 32, pp. 733-740
Stewart, J. C., Colorimetric determination of phospholipids with ammonium ferrothiocyanate (1980) Anal Biochem, 104, pp. 10-14
Zhu, Y. F., Chen, C., Recent advances in small molecule gonadotrophin-releasing hormone receptor antagonists (2004) Expert Opin Ther Pat, 14, pp. 187-199
Bombesin peptide antagonist for target-selective delivery of liposomal doxorubicin on cancer cells
Purpose: This study addresses novel peptide modified liposomal doxorubicin to specifically target tissues overexpressing bombesin (BN) receptors. Methods: DOTA-(AEEA)(2)-peptides containing the [7-14]bombesin and the new BN-AA1 sequence have been synthesized to compare their binding properties and in serum stabilities. The amphiphilic peptide derivative (MonY-BN-AA1) containing BN-AA1, a hydrophobic moiety, polyethylenglycole (PEG), and diethylenetriaminepentaacetate (DTPA), has been synthesized. Liposomes have been obtained by mixing of MonY-BN-AA1 with 1,2-distearoyl-sn-glycero-3-phosphocholine (DSPC). Results: Both In-111 labeled peptide derivatives present nanomolar Kd to PC-3 cells. Lu-177 labeled peptide DOTA-(AEEA)(2)-BN-AA1 is very stable (half-life 414.1 h), while DOTA-(AEEA)(2)-BN, shows a half-life of 15.5 h. In vivo studies on the therapeutic efficacy of DSPC/MonY-BN-AA1/Dox in comparison to DSPC/MonY-BN/Dox, were performed in PC-3 xenograft bearing mice. Both formulations showed similar tumor growth inhibition (TGI) compared to control animals treated with non-targeted DSPC/Dox liposomes or saline solution. For DSPC/MonY-BN-AA1/Dox the maximum effect was observed 19 days after treatment. Conclusions: DSPC/MonY-BN-AA1/Dox nanovectors confirm the ability to selectively target and provide therapeutic efficacy in mice. The lack of receptor activation and possible acute biological side effects provided by using the AA1 antagonist bombesin sequence should provide safe working conditions for further development of this class of drug delivery vehicles.
Purpose: This study addresses novel peptide modified liposomal doxorubicin to specifically target tissues overexpressing bombesin (BN) receptors. Methods: DOTA-(AEEA)(2)-peptides containing the [7-14]bombesin and the new BN-AA1 sequence have been synthesized to compare their binding properties and in serum stabilities. The amphiphilic peptide derivative (MonY-BN-AA1) containing BN-AA1, a hydrophobic moiety, polyethylenglycole (PEG), and diethylenetriaminepentaacetate (DTPA), has been synthesized. Liposomes have been obtained by mixing of MonY-BN-AA1 with 1,2-distearoyl-sn-glycero-3-phosphocholine (DSPC). Results: Both In-111 labeled peptide derivatives present nanomolar Kd to PC-3 cells. Lu-177 labeled peptide DOTA-(AEEA)(2)-BN-AA1 is very stable (half-life 414.1 h), while DOTA-(AEEA)(2)-BN, shows a half-life of 15.5 h. In vivo studies on the therapeutic efficacy of DSPC/MonY-BN-AA1/Dox in comparison to DSPC/MonY-BN/Dox, were performed in PC-3 xenograft bearing mice. Both formulations showed similar tumor growth inhibition (TGI) compared to control animals treated with non-targeted DSPC/Dox liposomes or saline solution. For DSPC/MonY-BN-AA1/Dox the maximum effect was observed 19 days after treatment. Conclusions: DSPC/MonY-BN-AA1/Dox nanovectors confirm the ability to selectively target and provide therapeutic efficacy in mice. The lack of receptor activation and possible acute biological side effects provided by using the AA1 antagonist bombesin sequence should provide safe working conditions for further development of this class of drug delivery vehicles.
Bombesin peptide antagonist for target-selective delivery of liposomal doxorubicin on cancer cells
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Bombesin peptide antagonist for target-selective delivery of liposomal doxorubicin on cancer cells
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Ringhieri P, Iannitti R, Nardon C, Palumbo R, Fregona D, Morelli G, Accardo A
* Target selective micelles for bombesin receptors incorporating Au(III)-dithiocarbamato complexes (473 views)
Int J Pharm (ISSN: 0378-5173, 1873-3476), 2014 Oct 1; 473(1-2): 194-202.
Impact Factor: 3.65
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Accardo A, Salsano G, Morisco A, Aurilio M, Parisi A, Maione F, Cicala C, Tesauro D, Aloj L, De Rosa G, Morelli G
* Peptide-modified liposomes for selective targeting of bombesin receptors overexpressed by cancer cells: A potential theranostic agent (381 views)
Int J Nanomed (ISSN: 1176-9114, 1178-2013, 1178-2013electronic), 2012; 7: 2007-2017.
Impact Factor: 3.463
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* Target selective micelles for bombesin receptors incorporating Au(III)-dithiocarbamato complexes (473 views)
Int J Pharm (ISSN: 0378-5173, 1873-3476), 2014 Oct 1; 473(1-2): 194-202.
Impact Factor: 3.65
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Accardo A, Salsano G, Morisco A, Aurilio M, Parisi A, Maione F, Cicala C, Tesauro D, Aloj L, De Rosa G, Morelli G
* Peptide-modified liposomes for selective targeting of bombesin receptors overexpressed by cancer cells: A potential theranostic agent (381 views)
Int J Nanomed (ISSN: 1176-9114, 1178-2013, 1178-2013electronic), 2012; 7: 2007-2017.
Impact Factor: 3.463
View Export to BibTeX Export to EndNote
2 Records (2 excluding Abstracts).
Total impact factor: 7.113 (7.113 excluding Abstracts).
Total 5 year impact factor: 8.038 (8.038 excluding Abstracts).
Total impact factor: 7.113 (7.113 excluding Abstracts).
Total 5 year impact factor: 8.038 (8.038 excluding Abstracts).
410 views. Last view on Saturday 14 January 2023, 17:17:01
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