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n3:pmcid: PMC0
bibo:doi: 10.1007%2Fs00259-010-1700-1
n5:contains: _:vb9760197 _:vb9760207 _:vb9760181

Subject Item: _:vb9760181
rdf:type: n5:Section
dc:title: introduction
n5:contains: _:vb9760182 _:vb9760183 _:vb9760184 _:vb9760185 _:vb9760186 _:vb9760187 _:vb9760188 _:vb9760189 _:vb9760190 _:vb9760191 _:vb9760192 _:vb9760193 _:vb9760194 _:vb9760195 _:vb9760196

Subject Item: _:vb9760182
rdf:type: n3:Context
rdf:value: Activation of EGFR causes signalling that may lead to cell division, increased motility, angiogenesis and suppression of apoptosis [>>1<<]. EGFR over-expression or constitutive activation has been shown to be associated with poor survival and recurrences in many human malignancies [2]. Detection of EGFR expression via nuclear medicine visualization may provide advantages
n3:mentions: n2:11252954

Subject Item: _:vb9760183
rdf:type: n3:Context
rdf:value: EGFR over-expression or constitutive activation has been shown to be associated with poor survival and recurrences in many human malignancies [>>2<<]. Detection of EGFR expression via nuclear medicine visualization may provide advantages over immunohistochemical staining of tumour biopsies, since evaluation of both the primary tumour as well as the metastases can be achieved. In
n3:mentions: n2:20130423

Subject Item: _:vb9760184
rdf:type: n3:Context
rdf:value: several studies with intact anti-EGFR (αEGFR) mAbs or mAb fragments labelled with single photon emission computed tomography (SPECT) (111In, 99mTc) or positron emission tomography (PET) (64Cu, 89Zr) radionuclides have been reported [>>3<<–9].
n3:mentions: n2:17262214 n2:19525473 n2:18454685 n2:12464779 n2:15471833 n2:8306274 n2:19091906

Subject Item: _:vb9760185
rdf:type: n3:Context
rdf:value: Nanobody technology provides new perspectives for mono- as well as multitarget tumour detection and therapy [>>10<<–12]. Nanobodies are derived from a unique antibody format that is present in species from the family of Camelidae, including llama, camel and dromedary.
n3:mentions: n2:18723476 n2:17694445

Subject Item: _:vb9760186
rdf:type: n3:Context
rdf:value: These animals contain, besides their conventional antibody repertoire, an antibody class consisting of heavy chains only [>>10<<, 13]. The variable region of the heavy-chain-only antibodies (VHH) represents the complete binding unit of the antibody. Because of the small size of these VHH fragments (∼15 kDa), this binding unit is also called Nanobody®. Although
n3:mentions: n2:17694445

Subject Item: _:vb9760187
rdf:type: n3:Context
rdf:value: These animals contain, besides their conventional antibody repertoire, an antibody class consisting of heavy chains only [10, >>13<<]. The variable region of the heavy-chain-only antibodies (VHH) represents the complete binding unit of the antibody. Because of the small size of these VHH fragments (∼15 kDa), this binding unit is also called Nanobody®. Although being
n3:mentions: n2:8502296

Subject Item: _:vb9760188
rdf:type: n3:Context
rdf:value: domain character, standard molecular biology techniques such as polymerase chain reaction (PCR) allow for the facile purification and selection of appropriate Nanobody candidates from the full antibody repertoire of immunized animals [>>14<<]. Unique features of the Nanobody technology platform in comparison to conventional mAb technology are easy and rapid drug development, and the easy and cheap production in bacteria and yeast [10, 15].
n3:mentions: n2:16738850

Subject Item: _:vb9760189
rdf:type: n3:Context
rdf:value: Unique features of the Nanobody technology platform in comparison to conventional mAb technology are easy and rapid drug development, and the easy and cheap production in bacteria and yeast [>>10<<, 15].
n3:mentions: n2:17694445

Subject Item: _:vb9760190
rdf:type: n3:Context
rdf:value: Unique features of the Nanobody technology platform in comparison to conventional mAb technology are easy and rapid drug development, and the easy and cheap production in bacteria and yeast [10, >>15<<].
n3:mentions: n2:11053416

Subject Item: _:vb9760191
rdf:type: n3:Context
rdf:value: For a proof of concept we used the Nanobody technology platform to construct two αEGFR Nanobodies [>>11<<]. The biodistribution of a 177Lu-labelled bivalent αEGFR Nanobody (αEGFR-αEGFR) in A431 tumour-bearing nude mice showed a tumour uptake of 5.0 ± 1.4 percentage of the injected dose per gram of tissue (%ID/g) at 6 h after injection and
n3:mentions: n2:18723476

Subject Item: _:vb9760192
rdf:type: n3:Context
rdf:value: The only clinically used BFC for 68Ga is 1,4,7,10-tetraazacyclododecane-N,N′,N″,N′″-tetraacetic acid (DOTA), but fast complex formation requires a high temperature [>>16<<–19]. More recently, several new chelates have been described for labelling of 68Ga to heat-labile proteins at ambient temperature including 1,4,7-triazacyclononane-1,4-7-triacetic acid (NOTA) and
n3:mentions: n2:19453100 n2:15820764 n2:15149183 n2:20175523

Subject Item: _:vb9760193
rdf:type: n3:Context
rdf:value: described for labelling of 68Ga to heat-labile proteins at ambient temperature including 1,4,7-triazacyclononane-1,4-7-triacetic acid (NOTA) and N,N′-bis[2-hydroxy-5-(carboxyethyl)benzyl]ethylenediamine-N,N′-diacetic acid (HBED-CC) [>>19<<–21]. However, this new generation of BFCs is not yet available for clinical immuno-PET applications.
n3:mentions: n2:20157706 n2:20175523 n2:18509635

Subject Item: _:vb9760194
rdf:type: n3:Context
rdf:value: For coupling of the long-lived positron emitter 89Zr (T ½ = 78.4 h, Eβ+max 0.9 MeV) (23%) to intact mAbs, we recently introduced the novel BFC p-isothiocyanatobenzyl derivative of desferrioxamine B (Df-Bz-NCS) [>>22<<, 23]. The choice of desferrioxamine B is attractive because it has been used safely in the clinical setting for many years.
n3:mentions: n2:19763566

Subject Item: _:vb9760195
rdf:type: n3:Context
rdf:value: For coupling of the long-lived positron emitter 89Zr (T ½ = 78.4 h, Eβ+max 0.9 MeV) (23%) to intact mAbs, we recently introduced the novel BFC p-isothiocyanatobenzyl derivative of desferrioxamine B (Df-Bz-NCS) [22, >>23<<]. The choice of desferrioxamine B is attractive because it has been used safely in the clinical setting for many years.
n3:mentions: n2:20360768

Subject Item: _:vb9760196
rdf:type: n3:Context
rdf:value: Since the hydroxamate function in desferrioxamine B has also been used for coupling of 67Ga in the past [>>24<<–27], we investigated whether this same Df-Bz-NCS can be used for labelling of 68Ga under mild conditions.
n3:mentions: n2:8295005 n2:15982582 n2:18383558 n2:2022990

Subject Item: _:vb9760197
rdf:type: n5:Section
dc:title: materials and methods
n5:contains: _:vb9760198 _:vb9760199 _:vb9760200 _:vb9760201 _:vb9760202 _:vb9760203 _:vb9760204 _:vb9760205 _:vb9760206

Subject Item: _:vb9760198
rdf:type: n3:Context
rdf:value: Nanobody 7D12 was generated by Ablynx NV (Ghent, Belgium) as described previously [>>14<<] and kindly provided to us.
n3:mentions: n2:16738850

Subject Item: _:vb9760199
rdf:type: n3:Context
rdf:value: The selection, production and characterization of chimeric mAb U36 (cmAb U36 11.53 mg/ml) directed against CD44v6 has been described elsewhere [>>28<<]. The human epidermoid cervical carcinoma cell line A431 was obtained from the American Type Culture Collection (www.atcc.com), ATCC number: CRL-1555. The head and neck squamous cell carcinoma (HNSCC) cell line UM-SCC-11B was obtained
n3:mentions: n2:8364934

Subject Item: _:vb9760200
rdf:type: n3:Context
rdf:value: T.E. Carey (Ann Arbor, MI, USA) [>>29<<]. 68Ga was obtained from a commercial 68Ge/68Ga generator based on a TiO2 bedding with 1.85 GBq 68Ge-loaded activity (IGG100; Eckert & Ziegler, Berlin, Germany).
n3:mentions: n2:9139877

Subject Item: _:vb9760201
rdf:type: n3:Context
rdf:value: The 68Ga was eluted from the 68Ge/68Ga generator as described by Velikyan et al. [>>16<<]. In short, the generator was eluted according to the manufacturer’s protocol with 3.5 ml ultra pure 0.1 M HCl solution.
n3:mentions: n2:15149183

Subject Item: _:vb9760202
rdf:type: n3:Context
rdf:value: cmAb U36 was premodified with Df-Bz-NCS as described by Perk et al. [>>22<<] (Fig. 1).
n3:mentions: n2:19763566

Subject Item: _:vb9760203
rdf:type: n3:Context
rdf:value: After PD-10 column purification the premodified 7D12 was labelled with 89Zr as described by Perk et al. [>>22<<]. In short, Df-Bz-NCS-7D12 (100–1,000 μg) was labelled with 89Zr (37 MBq) in 0.25 M HEPES buffer pH 7.0 at room temperature in a total volume of 2 ml. The 89Zr-Df-Bz-NCS-7D12 was purified by PD-10 column using 0.25 M NaOAc with 5 mg ml−1
n3:mentions: n2:19763566

Subject Item: _:vb9760204
rdf:type: n3:Context
rdf:value: determined by measuring the binding of the 68/67Ga-7D12 or 68/67Ga-cmAb U36 to a serial dilution of 2% paraformaldehyde fixed A431 cells or 0.2% glutaraldehyde fixed 11B cells, respectively, essentially as described by Lindmo et al. [>>30<<].
n3:mentions: n2:6086763

Subject Item: _:vb9760205
rdf:type: n3:Context
rdf:value: PET imaging was performed on a HRRT PET scanner (Siemens/CTI [>>31<<]), a dedicated human brain scanner. Three A431 xenograft-bearing mice were anaesthetized by inhalation of 2% isoflurane, injected with 5 MBq 68Ga-Df-Bz-NCS-7D12 (85 μg) via the retro-orbital plexus and scanned for 3 h.
n3:mentions: n2:17301468

Subject Item: _:vb9760206
rdf:type: n3:Context
rdf:value: For visualization of the images, the freely available Amide’s A Medical Imaging Data Examiner (AMIDE) program was used [>>32<<].
n3:mentions: n2:14649056

Subject Item: _:vb9760207
rdf:type: n5:Section
dc:title: discussion
n5:contains: _:vb9760216 _:vb9760217 _:vb9760218 _:vb9760219 _:vb9760220 _:vb9760221 _:vb9760222 _:vb9760223 _:vb9760208 _:vb9760209 _:vb9760210 _:vb9760211 _:vb9760212 _:vb9760213 _:vb9760214 _:vb9760215 _:vb9760240 _:vb9760241 _:vb9760232 _:vb9760233 _:vb9760234 _:vb9760235 _:vb9760236 _:vb9760237 _:vb9760238 _:vb9760239 _:vb9760224 _:vb9760225 _:vb9760226 _:vb9760227 _:vb9760228 _:vb9760229 _:vb9760230 _:vb9760231

Subject Item: _:vb9760208
rdf:type: n3:Context
rdf:value: In this study, we describe a method for labelling of αEFGR Nanobody 7D12 with 68Ga using the novel bifunctional desferal chelate (Df-Bz-NCS) which was previously introduced for the coupling of 89Zr to intact mAbs [>>22<<, 23]. Using this method, stable 68Ga-7D12 radioimmunoconjugates were produced as demonstrated by stability testing in storage buffer as well as in human serum with only slightly less stability as compared with the reference compound
n3:mentions: n2:19763566

Subject Item: _:vb9760209
rdf:type: n3:Context
rdf:value: In this study, we describe a method for labelling of αEFGR Nanobody 7D12 with 68Ga using the novel bifunctional desferal chelate (Df-Bz-NCS) which was previously introduced for the coupling of 89Zr to intact mAbs [22, >>23<<]. Using this method, stable 68Ga-7D12 radioimmunoconjugates were produced as demonstrated by stability testing in storage buffer as well as in human serum with only slightly less stability as compared with the reference compound
n3:mentions: n2:20360768

Subject Item: _:vb9760210
rdf:type: n3:Context
rdf:value: 89Zr-Df antibodies have been extensively evaluated in clinical immuno-PET studies [>>33<<].
n3:mentions: n2:20707716

Subject Item: _:vb9760211
rdf:type: n3:Context
rdf:value: and concentration of 68Ga by use of an anion exchange column, to further minimize the amounts of Al, Fe and Zr, to get rid of contaminating metals originating from the generator and to keep [68GaCl4−] volumes for labelling small [>>16<<, 34], (3) the addition of a highly concentrated NH4OAc solution to the [68GaCl4−] solution for efficient radiolabelling and stable complex formation (avoidance of the formation of gallium-oxo-chloro intermediates), (4) the use of a
n3:mentions: n2:15149183

Subject Item: _:vb9760212
rdf:type: n3:Context
rdf:value: and concentration of 68Ga by use of an anion exchange column, to further minimize the amounts of Al, Fe and Zr, to get rid of contaminating metals originating from the generator and to keep [68GaCl4−] volumes for labelling small [16, >>34<<], (3) the addition of a highly concentrated NH4OAc solution to the [68GaCl4−] solution for efficient radiolabelling and stable complex formation (avoidance of the formation of gallium-oxo-chloro intermediates), (4) the use of a
n3:mentions: n2:20117009

Subject Item: _:vb9760213
rdf:type: n3:Context
rdf:value: and stable complex formation (avoidance of the formation of gallium-oxo-chloro intermediates), (4) the use of a commercially available desferrioxamine B chelate that has been applied safely in the clinical setting for many years [>>23<<], (5) radiolabelling at room temperature within a relatively wide pH range of 5.0–6.5 and (6) the use of 0.25 M NaOAc with 5 mg ml−1 gentisic acid, pH 5.5 for protection during storage of the purified 68Ga-labelled conjugate.
n3:mentions: n2:20360768

Subject Item: _:vb9760214
rdf:type: n3:Context
rdf:value: The only chelate that has been used for 68Ga labelling of mAbs or mAb-like molecules for clinical purposes is DOTA [>>35<<]. With DOTA the best labelling kinetics were obtained in sodium acetate buffers at low pH [36].
n3:mentions: n2:20484419

Subject Item: _:vb9760215
rdf:type: n3:Context
rdf:value: With DOTA the best labelling kinetics were obtained in sodium acetate buffers at low pH [>>36<<]. Tolmachev et al. evaluated the 68Ga labelling kinetics of the DOTA-containing anti-HER2 Affibody ABY-002. Labelling at room temperature for 5 min appeared inefficient (decay-corrected yield of less than 5%). Only after elevation of the
n3:mentions: n2:20153401

Subject Item: _:vb9760216
rdf:type: n3:Context
rdf:value: binding and pharmacokinetic characteristics of this particular Affibody did not become affected upon labelling, but it is open to question whether other proteins can resist the harsh labelling conditions of low pH and high temperature [>>35<<, 37]. The same is true for microwave heating that has been used for labelling of DOTA bioconjugates with 68Ga [16, 38].
n3:mentions: n2:20484419

Subject Item: _:vb9760217
rdf:type: n3:Context
rdf:value: and pharmacokinetic characteristics of this particular Affibody did not become affected upon labelling, but it is open to question whether other proteins can resist the harsh labelling conditions of low pH and high temperature [35, >>37<<]. The same is true for microwave heating that has been used for labelling of DOTA bioconjugates with 68Ga [16, 38].
n3:mentions: n2:20130858

Subject Item: _:vb9760218
rdf:type: n3:Context
rdf:value: The same is true for microwave heating that has been used for labelling of DOTA bioconjugates with 68Ga [>>16<<, 38]. In our initial studies, using DOTA-Bz-NCS, less than 60% labelling was obtained after 20 min at 45°C, while the thus obtained labelled product was unstable. We postulate that at lower temperature no full N-coordination occurs. This
n3:mentions: n2:15149183

Subject Item: _:vb9760219
rdf:type: n3:Context
rdf:value: The same is true for microwave heating that has been used for labelling of DOTA bioconjugates with 68Ga [16, >>38<<]. In our initial studies, using DOTA-Bz-NCS, less than 60% labelling was obtained after 20 min at 45°C, while the thus obtained labelled product was unstable. We postulate that at lower temperature no full N-coordination occurs. This
n3:mentions: n2:16269603

Subject Item: _:vb9760220
rdf:type: n3:Context
rdf:value: This means that the 68Ga atom becomes ligated to the carboxyl functions of the DOTA molecule with still having water molecules in its coordination sphere instead of N, and that only concordant heating at elevated temperatures [>>37<<, 39] creates the additional N-coordination of the DOTA molecule leading to the 68Ga-DOTA complex that is suitable for in vivo applications.
n3:mentions: n2:20130858

Subject Item: _:vb9760221
rdf:type: n3:Context
rdf:value: This means that the 68Ga atom becomes ligated to the carboxyl functions of the DOTA molecule with still having water molecules in its coordination sphere instead of N, and that only concordant heating at elevated temperatures [37, >>39<<] creates the additional N-coordination of the DOTA molecule leading to the 68Ga-DOTA complex that is suitable for in vivo applications.
n3:mentions: n2:19690041

Subject Item: _:vb9760222
rdf:type: n3:Context
rdf:value: This important aspect of complex formation is fully analogous to what has been shown by us for the synthesis of the 186Re-MAG3 complex [>>40<<].
n3:mentions: n2:8229241

Subject Item: _:vb9760223
rdf:type: n3:Context
rdf:value: NOTA and its derivatives as well as the recently introduced HBED-CC chelates might have advantages over DOTA, since labelling with these chelates can be performed at room temperature and modest pH [>>19<<–21, 41]. These chelates, however, have not been clinically evaluated yet, and for us this was the reason to evaluate the desferrioxamine B derivative.
n3:mentions: n2:20157706 n2:20175523 n2:18509635

Subject Item: _:vb9760224
rdf:type: n3:Context
rdf:value: NOTA and its derivatives as well as the recently introduced HBED-CC chelates might have advantages over DOTA, since labelling with these chelates can be performed at room temperature and modest pH [19–21, >>41<<]. These chelates, however, have not been clinically evaluated yet, and for us this was the reason to evaluate the desferrioxamine B derivative.
n3:mentions: n2:18835159

Subject Item: _:vb9760225
rdf:type: n3:Context
rdf:value: The in vitro stability we found corresponds well with the earlier findings of Smith-Jones et al. [>>25<<], Fani et al. [27] and Furukawa et al. [24], but seems to be rather in contrast with the findings of Caraco et al. [42] and Govindan et al. [26].
n3:mentions: n2:8295005

Subject Item: _:vb9760226
rdf:type: n3:Context
rdf:value: The in vitro stability we found corresponds well with the earlier findings of Smith-Jones et al. [25], Fani et al. [>>27<<] and Furukawa et al. [24], but seems to be rather in contrast with the findings of Caraco et al. [42] and Govindan et al. [26].
n3:mentions: n2:18383558

Subject Item: _:vb9760227
rdf:type: n3:Context
rdf:value: The in vitro stability we found corresponds well with the earlier findings of Smith-Jones et al. [25], Fani et al. [27] and Furukawa et al. [>>24<<], but seems to be rather in contrast with the findings of Caraco et al. [42] and Govindan et al. [26].
n3:mentions: n2:2022990

Subject Item: _:vb9760228
rdf:type: n3:Context
rdf:value: The in vitro stability we found corresponds well with the earlier findings of Smith-Jones et al. [25], Fani et al. [27] and Furukawa et al. [24], but seems to be rather in contrast with the findings of Caraco et al. [>>42<<] and Govindan et al. [26].
n3:mentions: n2:9745687

Subject Item: _:vb9760229
rdf:type: n3:Context
rdf:value: vitro stability we found corresponds well with the earlier findings of Smith-Jones et al. [25], Fani et al. [27] and Furukawa et al. [24], but seems to be rather in contrast with the findings of Caraco et al. [42] and Govindan et al. [>>26<<]. We feel that this is only an apparent controversy because the conditions under which Caraco et al. produced their Ga-Df complex are completely different.
n3:mentions: n2:15982582

Subject Item: _:vb9760230
rdf:type: n3:Context
rdf:value: With respect to the findings of Govindan et al. [>>26<<], they already suggested themselves that their findings are most probably mixed up by the fact that the linkages between their mAb and Df are intrinsically instable.
n3:mentions: n2:15982582

Subject Item: _:vb9760231
rdf:type: n3:Context
rdf:value: Nuclear imaging techniques have a proven advantage over immunohistological techniques since nuclear imaging is noninvasive and whole-body scans can be obtained [>>43<<]. The use of Nanobodies as imaging moiety might have advantages over the use of intact mAbs, since a molecular weight of only 15 kDa allows for faster kinetics than intact mAbs in vivo. To our knowledge, Nanobodies have never been used
n3:mentions: n2:16728630

Subject Item: _:vb9760232
rdf:type: n3:Context
rdf:value: Huang et al. [>>44<<] and Gainkam et al. [45] studied the same (αEGFR) Nanobody 7D12 in the same A431 xenograft model, but labelled with 99mTc for SPECT applications.
n3:mentions: n2:18297364

Subject Item: _:vb9760233
rdf:type: n3:Context
rdf:value: Huang et al. [44] and Gainkam et al. [>>45<<] studied the same (αEGFR) Nanobody 7D12 in the same A431 xenograft model, but labelled with 99mTc for SPECT applications.
n3:mentions: n2:18413403

Subject Item: _:vb9760234
rdf:type: n3:Context
rdf:value: Given the superior properties of PET in comparison to SPECT for clinical quantitative imaging, these data suggest that 68Ga-7D12 is the more attractive Nanobody-based probe for assessment of EGFR expression [>>46<<, 47].
n3:mentions: n2:15653665

Subject Item: _:vb9760235
rdf:type: n3:Context
rdf:value: Given the superior properties of PET in comparison to SPECT for clinical quantitative imaging, these data suggest that 68Ga-7D12 is the more attractive Nanobody-based probe for assessment of EGFR expression [46, >>47<<].
n3:mentions: n2:19837762

Subject Item: _:vb9760236
rdf:type: n3:Context
rdf:value: with radiolabelled conventional intact mAbs used in other preclinical imaging studies. For example, in recent immuno-PET studies with 64Cu- and 89Zr-labelled anti-EGFR mAb cetuximab tumours could only be clearly delineated 16–24 h p.i. [>>7<<, 9, 48]. Another interesting small molecular protein was introduced for imaging of EGFR, namely the 8-kDa Affibody ZEGFR:
n3:mentions: n2:17262214

Subject Item: _:vb9760237
rdf:type: n3:Context
rdf:value: radiolabelled conventional intact mAbs used in other preclinical imaging studies. For example, in recent immuno-PET studies with 64Cu- and 89Zr-labelled anti-EGFR mAb cetuximab tumours could only be clearly delineated 16–24 h p.i. [7, >>9<<, 48]. Another interesting small molecular protein was introduced for imaging of EGFR, namely the 8-kDa Affibody ZEGFR:
n3:mentions: n2:19091906

Subject Item: _:vb9760238
rdf:type: n3:Context
rdf:value: conventional intact mAbs used in other preclinical imaging studies. For example, in recent immuno-PET studies with 64Cu- and 89Zr-labelled anti-EGFR mAb cetuximab tumours could only be clearly delineated 16–24 h p.i. [7, 9, >>48<<]. Another interesting small molecular protein was introduced for imaging of EGFR, namely the 8-kDa Affibody ZEGFR:
n3:mentions: n2:16269605

Subject Item: _:vb9760239
rdf:type: n3:Context
rdf:value: Another interesting small molecular protein was introduced for imaging of EGFR, namely the 8-kDa Affibody ZEGFR:2377 [>>49<<]. PET imaging studies in A431-bearing nude mice showed higher tumour contrast when 50 μg of 111In-labelled ZEGFR:2377 was injected in comparison to 5 μg, whereas for both doses high liver uptake was observed. For the 50 μg 111In-ZEGFR:
n3:mentions: n2:19838701

Subject Item: _:vb9760240
rdf:type: n3:Context
rdf:value: In accordance, initial clinical imaging studies with 111In-labelled anti-EGFR mAb 225 showed high liver uptake, requiring relatively high mAb doses for imaging of EGFR expression [>>50<<].
n3:mentions: n2:1988695

Subject Item: _:vb9760241
rdf:type: n3:Context
rdf:value: be easier for 68Ga-labelled Nanobodies directed against targets that show predominantly expression in the tumour, as was recently illustrated in PET imaging studies with 68Ga-labelled Affibody ABY-002 directed against the HER2 receptor [>>35<<].
n3:mentions: n2:20484419

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