Isolation of peptide ligands that interact specifically with human glioma cells

Poor prognosis of high grade gliomas coupled with the difficulty of widespread delivery of therapeutic agents prompted the search into new molecular targets. Our aim is to isolate glioma-specific peptide sequences that can be used for targeted delivery of therapeutic drugs and imaging tracer to accu...

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Bibliographic Details
Published in:Peptides (New York, N.Y. : 1980) Vol. 31; no. 4; pp. 644 - 650
Main Authors: Ho, Ivy A.W., Hui, Kam M., Lam, Paula Y.P.
Format: Journal Article
Language:English
Published: New York, NY Elsevier Inc 01.04.2010
Elsevier
Subjects:
Amino Acid Sequence
Biological and medical sciences
Cell Line, Tumor
Fundamental and applied biological sciences. Psychology
Glioma
Glioma - metabolism
Glioma - pathology
Glioma-specific
Humans
Ligands
Medical sciences
Molecular Sequence Data
Neoplasm Transplantation
Neurology
Peptides - genetics
Peptides - isolation & purification
Peptides - metabolism
Phage display
Tissue Distribution
Transplantation, Heterologous
Tumors of the nervous system. Phacomatoses
Vector targeting
Vertebrates: endocrinology
Vector targeting
Phage display
Glioma-specific
Glioma
Human
Nervous system diseases
Targeting
Peptides
Ligand
Cell line
Central nervous system disease
Tumor
Isolation
Vector
ISSN:0196-9781, 1873-5169, 1873-5169
Online Access:Get full text
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Description
Summary:Poor prognosis of high grade gliomas coupled with the difficulty of widespread delivery of therapeutic agents prompted the search into new molecular targets. Our aim is to isolate glioma-specific peptide sequences that can be used for targeted delivery of therapeutic drugs and imaging tracer to accurately demarcate tumor volume as a response to therapy. Herein, we describe the isolation and characterization of a glioma-specific peptide sequence, GL1, that interact exclusively with human glioma cells lines and primary glioma cells derived from human biopsy in vitro. Further analysis showed that the receptors for GL1 were located on the external side of the plasma membrane, where the GL1 peptides could bind stably up to a period of 180 min. More importantly, GL1 phages home specifically to human glioma xenograft when administered through tail vein, a phenomenon that was not observed when non-specific phages were used as control. Taken together, our results confirmed that GL1 could represent a novel peptide that target to tumor of glial origins, and could potentially be used as a targeting moiety for the conjugation of therapeutic drugs or diagnostic imaging radiolabels.
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ISSN:0196-9781
1873-5169
1873-5169
DOI:10.1016/j.peptides.2009.12.020