1995
DOI: 10.1016/s0140-6736(95)92839-1
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Breast cancer imaging with radiolabelled peptide from complementarity-determining region of antitumour antibody

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Cited by 44 publications
(32 citation statements)
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“…Consequently, the use of small peptides instead may eliminate these shortcomings because peptide ligands are nonimmunogenic and have high affinity and selectivity for receptors. In this study, we used a synthetic peptide, designated EPPT1 (YCAREPPTRTFAYWG), derived from the CDR3 V h region of a monoclonal antibody (ASM2) raised against human epithelial cancer cells (25,31). Analysis of peptide structure revealed a ␤-strand type conformation as the active binding site (32).…”
Section: Introductionmentioning
confidence: 99%
See 1 more Smart Citation
“…Consequently, the use of small peptides instead may eliminate these shortcomings because peptide ligands are nonimmunogenic and have high affinity and selectivity for receptors. In this study, we used a synthetic peptide, designated EPPT1 (YCAREPPTRTFAYWG), derived from the CDR3 V h region of a monoclonal antibody (ASM2) raised against human epithelial cancer cells (25,31). Analysis of peptide structure revealed a ␤-strand type conformation as the active binding site (32).…”
Section: Introductionmentioning
confidence: 99%
“…1A). In a previous study, the EPPT1 peptide, labeled with ( 99m Tc), was used to image breast carcinomas in vivo (31).…”
Section: Introductionmentioning
confidence: 99%
“…consequently, the use of small peptides instead of antibodies or antibody fragments may eliminate these shortcomings, because peptide ligands are nonimmunogenic and combine high affinity and selectivity for receptors with more desirable pharmacokinetic properties. in our studies we have traditionally used a synthetic peptide, ePPt1 (YcARePPtRtFAYWG), derived from the cDR3 V h region of a monoclonal antibody (ASM2) raised against human epithelial cancer cells (30,84). Analysis of the peptide structure revealed a b-strand type portion of the sequence as the active binding site (31).…”
Section: Imaging Target-umuc-1 Tumor Antigenmentioning
confidence: 99%
“…that property of the APDtRP sequence is the basis for its exclusive immunogenicity in the underglycosylated mucin-1 protein (17). in a previous study, the ePPt1 peptide, labeled with ( 99m tc), was used to image breast carcinomas in vivo (84). the 99m tc -labeled ePPt1 peptide is the basis for a commercially developed breast cancer imaging agent.…”
Section: Imaging Target-umuc-1 Tumor Antigenmentioning
confidence: 99%
“…Moreover, a hydrophilic conjugate with predominant kidney excretion has to be prepared. High kidney retention of the peptides and antibody fragments -labelled with a metallic radionuclide -appeared to be one of the main obstacles in the potential use of small molecules in internal radiotherapy [3]. Therefore, we have developed a new chelator somatostatin analogue which can be labelled stably with the diagnostic radionuclide 111In and its therapeutic chemical analogue 90y.…”
Section: Introductionmentioning
confidence: 99%