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• W2045227238 abstract "Agouti-related protein (AgRP) is a 4-kDa cystine-knot peptide of human origin with four disulfide bonds and four solvent-exposed loops. The cell adhesion receptor integrin<mml:math xmlns:mml=http://www.w3.org/1998/Math/MathML><mml:msub><mml:mi>α</mml:mi><mml:mtext>v</mml:mtext></mml:msub><mml:msub><mml:mi>β</mml:mi><mml:mn>3</mml:mn></mml:msub></mml:math>is an important tumor angiogenesis factor that determines the invasiveness and metastatic ability of many malignant tumors. AgRP mutants have been engineered to bind to integrin<mml:math xmlns:mml=http://www.w3.org/1998/Math/MathML><mml:msub><mml:mi>α</mml:mi><mml:mtext>v</mml:mtext></mml:msub><mml:msub><mml:mi>β</mml:mi><mml:mn>3</mml:mn></mml:msub></mml:math>with high affinity and specificity using directed evolution. Here, AgRP mutants 7C and 6E were radiolabeled with 111 In and evaluated for in vivo targeting of tumor integrin<mml:math xmlns:mml=http://www.w3.org/1998/Math/MathML><mml:msub><mml:mi>α</mml:mi><mml:mtext>v</mml:mtext></mml:msub><mml:msub><mml:mi>β</mml:mi><mml:mn>3</mml:mn></mml:msub></mml:math>receptors. AgRP peptides were conjugated to the metal chelator 1, 4, 7, 10-tetra-azacyclododecane- N,<mml:math xmlns:mml=http://www.w3.org/1998/Math/MathML><mml:msup><mml:mtext>N</mml:mtext><mml:mo>′</mml:mo></mml:msup></mml:math>,<mml:math xmlns:mml=http://www.w3.org/1998/Math/MathML><mml:msup><mml:mtext>N</mml:mtext><mml:mo>″</mml:mo></mml:msup></mml:math>,<mml:math xmlns:mml=http://www.w3.org/1998/Math/MathML><mml:msup><mml:mtext>N</mml:mtext><mml:mo>‴</mml:mo></mml:msup></mml:math>-tetraacetic acid (DOTA) and radiolabeled with 111 In. The stability of the radiopeptides 111 In-DOTA-AgRP-7C and 111 In-DOTA-AgRP-6E was tested in phosphate-buffered saline (PBS) and mouse serum, respectively. Cell uptake assays of the radiolabeled peptides were performed in U87MG cell lines. Biodistribution studies were performed to evaluate the in vivo performance of the two resulting probes using mice bearing integrin-expressing U87MG xenograft tumors. Both AgRP peptides were easily labeled with 111 In in high yield and radiochemical purity (>99%). The two probes exhibited high stability in phosphate-buffered saline and mouse serum. Compared with 111 In-DOTA-AgRP-6E, 111 In-DOTA-AgRP-7C showed increased U87MG tumor uptake and longer tumor retention (<mml:math xmlns:mml=http://www.w3.org/1998/Math/MathML><mml:mn>5.74</mml:mn><mml:mo>±</mml:mo><mml:mn>1.60</mml:mn></mml:math>and<mml:math xmlns:mml=http://www.w3.org/1998/Math/MathML><mml:mn>1.29</mml:mn><mml:mo>±</mml:mo><mml:mn>0.02</mml:mn></mml:math>%ID/g at 0.5 and 24 h, resp.), which was consistent with measurements of cell uptake. Moreover, the tumor uptake of 111 In-DOTA-AgRP-7C was specifically inhibited by coinjection with an excess of the integrin-binding peptidomimetic c(RGDyK). Thus, 111 In-DOTA-AgRP-7C is a promising probe for targeting integrin<mml:math xmlns:mml=http://www.w3.org/1998/Math/MathML><mml:msub><mml:mi>α</mml:mi><mml:mtext>v</mml:mtext></mml:msub><mml:msub><mml:mi>β</mml:mi><mml:mn>3</mml:mn></mml:msub></mml:math>positive tumors in living subjects." @default.
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• W2045227238 date "2012-01-01" @default.
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• W2045227238 title "<mml:math xmlns:mml=http://www.w3.org/1998/Math/MathML><mml:mtext>I</mml:mtext><mml:mrow><mml:mtext>111</mml:mtext></mml:mrow><mml:mtext>n</mml:mtext></mml:math>-Labeled Cystine-Knot Peptides Based on the Agouti-Related Protein for Targeting Tumor Angiogenesis" @default.
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• W2045227238 doi "https://doi.org/10.1155/2012/368075" @default.
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