The Experts below are selected from a list of 193467 Experts worldwide ranked by ideXlab platform
In Seop Chang - One of the best experts on this subject based on the ideXlab platform.
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biosensing and electrochemical properties of flavin adenine dinucleotide fad dependent glucose dehydrogenase gdh fused to a gold Binding Peptide
Biosensors and Bioelectronics, 2020Co-Authors: Hyeryeong Lee, Seungwoo Baek, Stacy Simai Reginald, Ingeol Choi, Yoo Seok Lee, Eun Mi Lee, In Seop ChangAbstract:In the present work, direct electron transfer (DET) based biosensing system for the determination of glucose has been fabricated by utilizing gold Binding Peptide (GBP) fused flavin adenine dinucleotide-dependent glucose dehydrogenase (FAD-GDH) from Burkholderia cepacia. The GBP fused FAD-GDH was immobilized on the working electrode surface of screen-printed electrode (SPE) which consists of gold working electrode, a silver pseudo-reference electrode and a platinum counter electrode, to develop the biosensing system with compact design and favorable sensing ability. The bioelectrochemical and mechanical properties of GBP fused FAD-GDH (GDH-GBP) immobilized SPE (GDH-GBP/Au) were investigated. Here, the Binding affinity of GDH-GBP on Au surface, was highly increased after fusion of gold Binding Peptide and its uniform monolayer was formed on Au surface. In the cyclic voltammetry (CV), GDH-GBP/Au displayed significantly high oxidative peak currents corresponding to glucose oxidation which is almost c.a. 10-fold enhanced value compared with that from native GDH immobilized SPE (GDH/Au). As well, GDH-GBP/Au has shown 92.37% of current retention after successive potential scans. In the chronoamperometry, its steady-state catalytic current was monitored in various conditions. The dynamic range of GDH-GBP/Au was shown to be 3-30 mM at 30 °C and exhibits high selectivity toward glucose in whole human blood. Additionally, temperature dependency of GDH-GBP/Au on DET capability was also investigated at 30-70 °C. Considering this efficient and stable glucose sensing with simple and easy sensor fabrication, GDH-GBP based sensing platform can provide new insight for future biosensor in research fields that rely on DET.
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construction of uniform monolayer and orientation tunable enzyme electrode by a synthetic glucose dehydrogenase without electron transfer subunit via optimized site specific gold Binding Peptide capable of direct electron transfer
ACS Applied Materials & Interfaces, 2018Co-Authors: Seungwoo Baek, Stacy Simai Reginald, Hyunsoo Kang, Ingeol Choi, In Seop ChangAbstract:Direct electron transfer (DET) between enzymes and electrodes is a key issue for practical use of bioelectrocatalytic devices as a bioenergy process, such as enzymatic electrosynthesis, biosensors, and enzyme biofuel cells. To date, based on the DET of bioelectrocatalysis, less than 1% of the calculated theoretical current was transferred to final electron acceptor due to energy loss at enzyme–electrode interface. This study describes the design and construction of a synthetic glucose dehydrogenase (GDH; α and γ subunits) combined with a gold-Binding Peptide at its amino or carboxy terminus for direct contact between enzyme and electrode. The fused gold-Binding Peptide facilitated stable immobilization of GDH and constructed uniform monolayer of GDH onto a Au electrode. Depending on the fused site of Binding Peptide to the enzyme complex, nine combinations of recombinant GDH proteins on the electrode show significantly different direct electron-transfer efficiency across the enzyme–electrode interface. Th...
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Construction of Uniform Monolayer- and Orientation-Tunable Enzyme Electrode by a Synthetic Glucose Dehydrogenase without Electron-Transfer Subunit via Optimized Site-Specific Gold-Binding Peptide Capable of Direct Electron Transfer
2018Co-Authors: Yoo Seok Lee, Seungwoo Baek, Stacy Simai Reginald, Hyunsoo Kang, Ingeol Choi, Hyeryeong Lee, Yeongeun Kim, In Seop ChangAbstract:Direct electron transfer (DET) between enzymes and electrodes is a key issue for practical use of bioelectrocatalytic devices as a bioenergy process, such as enzymatic electrosynthesis, biosensors, and enzyme biofuel cells. To date, based on the DET of bioelectrocatalysis, less than 1% of the calculated theoretical current was transferred to final electron acceptor due to energy loss at enzyme–electrode interface. This study describes the design and construction of a synthetic glucose dehydrogenase (GDH; α and γ subunits) combined with a gold-Binding Peptide at its amino or carboxy terminus for direct contact between enzyme and electrode. The fused gold-Binding Peptide facilitated stable immobilization of GDH and constructed uniform monolayer of GDH onto a Au electrode. Depending on the fused site of Binding Peptide to the enzyme complex, nine combinations of recombinant GDH proteins on the electrode show significantly different direct electron-transfer efficiency across the enzyme–electrode interface. The fusion of site-specific Binding Peptide to the catalytic subunit (α subunit, carboxy terminus) of the enzyme complex enabled apparent direct electron transfer (DET) across the enzyme–electrode interface even in the absence of the electron-transfer subunit (i.e., β subunit having cytochrome domain). The catalytic glucose oxidation current at an onset potential of ca. (−)0.46 V vs Ag/AgCl was associated with the appearance of an flavin adenine dinucleotide (FAD)/FADH2 redox wave and a stabilized bioelectrocatalytic current of more than 100 μA, determined from chronoamperometric analysis. Electron recovery was 7.64%, and the catalytic current generation was 249 μA per GDH enzyme loading unit (U), several orders of magnitude higher than the values reported previously. These observations corroborated that the last electron donor facing to electrode was controlled to be in close proximity without electron-transfer intermediates and the native affinity for glucose was preserved. The design and construction of the site-specific “sticky-ended” proteins without loss of catalytic activity could be applied to other redox enzymes having a buried active site
Seungwoo Baek - One of the best experts on this subject based on the ideXlab platform.
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biosensing and electrochemical properties of flavin adenine dinucleotide fad dependent glucose dehydrogenase gdh fused to a gold Binding Peptide
Biosensors and Bioelectronics, 2020Co-Authors: Hyeryeong Lee, Seungwoo Baek, Stacy Simai Reginald, Ingeol Choi, Yoo Seok Lee, Eun Mi Lee, In Seop ChangAbstract:In the present work, direct electron transfer (DET) based biosensing system for the determination of glucose has been fabricated by utilizing gold Binding Peptide (GBP) fused flavin adenine dinucleotide-dependent glucose dehydrogenase (FAD-GDH) from Burkholderia cepacia. The GBP fused FAD-GDH was immobilized on the working electrode surface of screen-printed electrode (SPE) which consists of gold working electrode, a silver pseudo-reference electrode and a platinum counter electrode, to develop the biosensing system with compact design and favorable sensing ability. The bioelectrochemical and mechanical properties of GBP fused FAD-GDH (GDH-GBP) immobilized SPE (GDH-GBP/Au) were investigated. Here, the Binding affinity of GDH-GBP on Au surface, was highly increased after fusion of gold Binding Peptide and its uniform monolayer was formed on Au surface. In the cyclic voltammetry (CV), GDH-GBP/Au displayed significantly high oxidative peak currents corresponding to glucose oxidation which is almost c.a. 10-fold enhanced value compared with that from native GDH immobilized SPE (GDH/Au). As well, GDH-GBP/Au has shown 92.37% of current retention after successive potential scans. In the chronoamperometry, its steady-state catalytic current was monitored in various conditions. The dynamic range of GDH-GBP/Au was shown to be 3-30 mM at 30 °C and exhibits high selectivity toward glucose in whole human blood. Additionally, temperature dependency of GDH-GBP/Au on DET capability was also investigated at 30-70 °C. Considering this efficient and stable glucose sensing with simple and easy sensor fabrication, GDH-GBP based sensing platform can provide new insight for future biosensor in research fields that rely on DET.
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construction of uniform monolayer and orientation tunable enzyme electrode by a synthetic glucose dehydrogenase without electron transfer subunit via optimized site specific gold Binding Peptide capable of direct electron transfer
ACS Applied Materials & Interfaces, 2018Co-Authors: Seungwoo Baek, Stacy Simai Reginald, Hyunsoo Kang, Ingeol Choi, In Seop ChangAbstract:Direct electron transfer (DET) between enzymes and electrodes is a key issue for practical use of bioelectrocatalytic devices as a bioenergy process, such as enzymatic electrosynthesis, biosensors, and enzyme biofuel cells. To date, based on the DET of bioelectrocatalysis, less than 1% of the calculated theoretical current was transferred to final electron acceptor due to energy loss at enzyme–electrode interface. This study describes the design and construction of a synthetic glucose dehydrogenase (GDH; α and γ subunits) combined with a gold-Binding Peptide at its amino or carboxy terminus for direct contact between enzyme and electrode. The fused gold-Binding Peptide facilitated stable immobilization of GDH and constructed uniform monolayer of GDH onto a Au electrode. Depending on the fused site of Binding Peptide to the enzyme complex, nine combinations of recombinant GDH proteins on the electrode show significantly different direct electron-transfer efficiency across the enzyme–electrode interface. Th...
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Construction of Uniform Monolayer- and Orientation-Tunable Enzyme Electrode by a Synthetic Glucose Dehydrogenase without Electron-Transfer Subunit via Optimized Site-Specific Gold-Binding Peptide Capable of Direct Electron Transfer
2018Co-Authors: Yoo Seok Lee, Seungwoo Baek, Stacy Simai Reginald, Hyunsoo Kang, Ingeol Choi, Hyeryeong Lee, Yeongeun Kim, In Seop ChangAbstract:Direct electron transfer (DET) between enzymes and electrodes is a key issue for practical use of bioelectrocatalytic devices as a bioenergy process, such as enzymatic electrosynthesis, biosensors, and enzyme biofuel cells. To date, based on the DET of bioelectrocatalysis, less than 1% of the calculated theoretical current was transferred to final electron acceptor due to energy loss at enzyme–electrode interface. This study describes the design and construction of a synthetic glucose dehydrogenase (GDH; α and γ subunits) combined with a gold-Binding Peptide at its amino or carboxy terminus for direct contact between enzyme and electrode. The fused gold-Binding Peptide facilitated stable immobilization of GDH and constructed uniform monolayer of GDH onto a Au electrode. Depending on the fused site of Binding Peptide to the enzyme complex, nine combinations of recombinant GDH proteins on the electrode show significantly different direct electron-transfer efficiency across the enzyme–electrode interface. The fusion of site-specific Binding Peptide to the catalytic subunit (α subunit, carboxy terminus) of the enzyme complex enabled apparent direct electron transfer (DET) across the enzyme–electrode interface even in the absence of the electron-transfer subunit (i.e., β subunit having cytochrome domain). The catalytic glucose oxidation current at an onset potential of ca. (−)0.46 V vs Ag/AgCl was associated with the appearance of an flavin adenine dinucleotide (FAD)/FADH2 redox wave and a stabilized bioelectrocatalytic current of more than 100 μA, determined from chronoamperometric analysis. Electron recovery was 7.64%, and the catalytic current generation was 249 μA per GDH enzyme loading unit (U), several orders of magnitude higher than the values reported previously. These observations corroborated that the last electron donor facing to electrode was controlled to be in close proximity without electron-transfer intermediates and the native affinity for glucose was preserved. The design and construction of the site-specific “sticky-ended” proteins without loss of catalytic activity could be applied to other redox enzymes having a buried active site
Ingeol Choi - One of the best experts on this subject based on the ideXlab platform.
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biosensing and electrochemical properties of flavin adenine dinucleotide fad dependent glucose dehydrogenase gdh fused to a gold Binding Peptide
Biosensors and Bioelectronics, 2020Co-Authors: Hyeryeong Lee, Seungwoo Baek, Stacy Simai Reginald, Ingeol Choi, Yoo Seok Lee, Eun Mi Lee, In Seop ChangAbstract:In the present work, direct electron transfer (DET) based biosensing system for the determination of glucose has been fabricated by utilizing gold Binding Peptide (GBP) fused flavin adenine dinucleotide-dependent glucose dehydrogenase (FAD-GDH) from Burkholderia cepacia. The GBP fused FAD-GDH was immobilized on the working electrode surface of screen-printed electrode (SPE) which consists of gold working electrode, a silver pseudo-reference electrode and a platinum counter electrode, to develop the biosensing system with compact design and favorable sensing ability. The bioelectrochemical and mechanical properties of GBP fused FAD-GDH (GDH-GBP) immobilized SPE (GDH-GBP/Au) were investigated. Here, the Binding affinity of GDH-GBP on Au surface, was highly increased after fusion of gold Binding Peptide and its uniform monolayer was formed on Au surface. In the cyclic voltammetry (CV), GDH-GBP/Au displayed significantly high oxidative peak currents corresponding to glucose oxidation which is almost c.a. 10-fold enhanced value compared with that from native GDH immobilized SPE (GDH/Au). As well, GDH-GBP/Au has shown 92.37% of current retention after successive potential scans. In the chronoamperometry, its steady-state catalytic current was monitored in various conditions. The dynamic range of GDH-GBP/Au was shown to be 3-30 mM at 30 °C and exhibits high selectivity toward glucose in whole human blood. Additionally, temperature dependency of GDH-GBP/Au on DET capability was also investigated at 30-70 °C. Considering this efficient and stable glucose sensing with simple and easy sensor fabrication, GDH-GBP based sensing platform can provide new insight for future biosensor in research fields that rely on DET.
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construction of uniform monolayer and orientation tunable enzyme electrode by a synthetic glucose dehydrogenase without electron transfer subunit via optimized site specific gold Binding Peptide capable of direct electron transfer
ACS Applied Materials & Interfaces, 2018Co-Authors: Seungwoo Baek, Stacy Simai Reginald, Hyunsoo Kang, Ingeol Choi, In Seop ChangAbstract:Direct electron transfer (DET) between enzymes and electrodes is a key issue for practical use of bioelectrocatalytic devices as a bioenergy process, such as enzymatic electrosynthesis, biosensors, and enzyme biofuel cells. To date, based on the DET of bioelectrocatalysis, less than 1% of the calculated theoretical current was transferred to final electron acceptor due to energy loss at enzyme–electrode interface. This study describes the design and construction of a synthetic glucose dehydrogenase (GDH; α and γ subunits) combined with a gold-Binding Peptide at its amino or carboxy terminus for direct contact between enzyme and electrode. The fused gold-Binding Peptide facilitated stable immobilization of GDH and constructed uniform monolayer of GDH onto a Au electrode. Depending on the fused site of Binding Peptide to the enzyme complex, nine combinations of recombinant GDH proteins on the electrode show significantly different direct electron-transfer efficiency across the enzyme–electrode interface. Th...
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Construction of Uniform Monolayer- and Orientation-Tunable Enzyme Electrode by a Synthetic Glucose Dehydrogenase without Electron-Transfer Subunit via Optimized Site-Specific Gold-Binding Peptide Capable of Direct Electron Transfer
2018Co-Authors: Yoo Seok Lee, Seungwoo Baek, Stacy Simai Reginald, Hyunsoo Kang, Ingeol Choi, Hyeryeong Lee, Yeongeun Kim, In Seop ChangAbstract:Direct electron transfer (DET) between enzymes and electrodes is a key issue for practical use of bioelectrocatalytic devices as a bioenergy process, such as enzymatic electrosynthesis, biosensors, and enzyme biofuel cells. To date, based on the DET of bioelectrocatalysis, less than 1% of the calculated theoretical current was transferred to final electron acceptor due to energy loss at enzyme–electrode interface. This study describes the design and construction of a synthetic glucose dehydrogenase (GDH; α and γ subunits) combined with a gold-Binding Peptide at its amino or carboxy terminus for direct contact between enzyme and electrode. The fused gold-Binding Peptide facilitated stable immobilization of GDH and constructed uniform monolayer of GDH onto a Au electrode. Depending on the fused site of Binding Peptide to the enzyme complex, nine combinations of recombinant GDH proteins on the electrode show significantly different direct electron-transfer efficiency across the enzyme–electrode interface. The fusion of site-specific Binding Peptide to the catalytic subunit (α subunit, carboxy terminus) of the enzyme complex enabled apparent direct electron transfer (DET) across the enzyme–electrode interface even in the absence of the electron-transfer subunit (i.e., β subunit having cytochrome domain). The catalytic glucose oxidation current at an onset potential of ca. (−)0.46 V vs Ag/AgCl was associated with the appearance of an flavin adenine dinucleotide (FAD)/FADH2 redox wave and a stabilized bioelectrocatalytic current of more than 100 μA, determined from chronoamperometric analysis. Electron recovery was 7.64%, and the catalytic current generation was 249 μA per GDH enzyme loading unit (U), several orders of magnitude higher than the values reported previously. These observations corroborated that the last electron donor facing to electrode was controlled to be in close proximity without electron-transfer intermediates and the native affinity for glucose was preserved. The design and construction of the site-specific “sticky-ended” proteins without loss of catalytic activity could be applied to other redox enzymes having a buried active site
Stacy Simai Reginald - One of the best experts on this subject based on the ideXlab platform.
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biosensing and electrochemical properties of flavin adenine dinucleotide fad dependent glucose dehydrogenase gdh fused to a gold Binding Peptide
Biosensors and Bioelectronics, 2020Co-Authors: Hyeryeong Lee, Seungwoo Baek, Stacy Simai Reginald, Ingeol Choi, Yoo Seok Lee, Eun Mi Lee, In Seop ChangAbstract:In the present work, direct electron transfer (DET) based biosensing system for the determination of glucose has been fabricated by utilizing gold Binding Peptide (GBP) fused flavin adenine dinucleotide-dependent glucose dehydrogenase (FAD-GDH) from Burkholderia cepacia. The GBP fused FAD-GDH was immobilized on the working electrode surface of screen-printed electrode (SPE) which consists of gold working electrode, a silver pseudo-reference electrode and a platinum counter electrode, to develop the biosensing system with compact design and favorable sensing ability. The bioelectrochemical and mechanical properties of GBP fused FAD-GDH (GDH-GBP) immobilized SPE (GDH-GBP/Au) were investigated. Here, the Binding affinity of GDH-GBP on Au surface, was highly increased after fusion of gold Binding Peptide and its uniform monolayer was formed on Au surface. In the cyclic voltammetry (CV), GDH-GBP/Au displayed significantly high oxidative peak currents corresponding to glucose oxidation which is almost c.a. 10-fold enhanced value compared with that from native GDH immobilized SPE (GDH/Au). As well, GDH-GBP/Au has shown 92.37% of current retention after successive potential scans. In the chronoamperometry, its steady-state catalytic current was monitored in various conditions. The dynamic range of GDH-GBP/Au was shown to be 3-30 mM at 30 °C and exhibits high selectivity toward glucose in whole human blood. Additionally, temperature dependency of GDH-GBP/Au on DET capability was also investigated at 30-70 °C. Considering this efficient and stable glucose sensing with simple and easy sensor fabrication, GDH-GBP based sensing platform can provide new insight for future biosensor in research fields that rely on DET.
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construction of uniform monolayer and orientation tunable enzyme electrode by a synthetic glucose dehydrogenase without electron transfer subunit via optimized site specific gold Binding Peptide capable of direct electron transfer
ACS Applied Materials & Interfaces, 2018Co-Authors: Seungwoo Baek, Stacy Simai Reginald, Hyunsoo Kang, Ingeol Choi, In Seop ChangAbstract:Direct electron transfer (DET) between enzymes and electrodes is a key issue for practical use of bioelectrocatalytic devices as a bioenergy process, such as enzymatic electrosynthesis, biosensors, and enzyme biofuel cells. To date, based on the DET of bioelectrocatalysis, less than 1% of the calculated theoretical current was transferred to final electron acceptor due to energy loss at enzyme–electrode interface. This study describes the design and construction of a synthetic glucose dehydrogenase (GDH; α and γ subunits) combined with a gold-Binding Peptide at its amino or carboxy terminus for direct contact between enzyme and electrode. The fused gold-Binding Peptide facilitated stable immobilization of GDH and constructed uniform monolayer of GDH onto a Au electrode. Depending on the fused site of Binding Peptide to the enzyme complex, nine combinations of recombinant GDH proteins on the electrode show significantly different direct electron-transfer efficiency across the enzyme–electrode interface. Th...
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Construction of Uniform Monolayer- and Orientation-Tunable Enzyme Electrode by a Synthetic Glucose Dehydrogenase without Electron-Transfer Subunit via Optimized Site-Specific Gold-Binding Peptide Capable of Direct Electron Transfer
2018Co-Authors: Yoo Seok Lee, Seungwoo Baek, Stacy Simai Reginald, Hyunsoo Kang, Ingeol Choi, Hyeryeong Lee, Yeongeun Kim, In Seop ChangAbstract:Direct electron transfer (DET) between enzymes and electrodes is a key issue for practical use of bioelectrocatalytic devices as a bioenergy process, such as enzymatic electrosynthesis, biosensors, and enzyme biofuel cells. To date, based on the DET of bioelectrocatalysis, less than 1% of the calculated theoretical current was transferred to final electron acceptor due to energy loss at enzyme–electrode interface. This study describes the design and construction of a synthetic glucose dehydrogenase (GDH; α and γ subunits) combined with a gold-Binding Peptide at its amino or carboxy terminus for direct contact between enzyme and electrode. The fused gold-Binding Peptide facilitated stable immobilization of GDH and constructed uniform monolayer of GDH onto a Au electrode. Depending on the fused site of Binding Peptide to the enzyme complex, nine combinations of recombinant GDH proteins on the electrode show significantly different direct electron-transfer efficiency across the enzyme–electrode interface. The fusion of site-specific Binding Peptide to the catalytic subunit (α subunit, carboxy terminus) of the enzyme complex enabled apparent direct electron transfer (DET) across the enzyme–electrode interface even in the absence of the electron-transfer subunit (i.e., β subunit having cytochrome domain). The catalytic glucose oxidation current at an onset potential of ca. (−)0.46 V vs Ag/AgCl was associated with the appearance of an flavin adenine dinucleotide (FAD)/FADH2 redox wave and a stabilized bioelectrocatalytic current of more than 100 μA, determined from chronoamperometric analysis. Electron recovery was 7.64%, and the catalytic current generation was 249 μA per GDH enzyme loading unit (U), several orders of magnitude higher than the values reported previously. These observations corroborated that the last electron donor facing to electrode was controlled to be in close proximity without electron-transfer intermediates and the native affinity for glucose was preserved. The design and construction of the site-specific “sticky-ended” proteins without loss of catalytic activity could be applied to other redox enzymes having a buried active site
Erwann Guénin - One of the best experts on this subject based on the ideXlab platform.
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USPIO–PEG nanoparticles functionalized with a highly specific collagen-Binding Peptide: a step towards MRI diagnosis of fibrosis
Journal of materials chemistry B, 2020Co-Authors: Hanene Belkahla, Joana Antunes, Yoann Lalatonne, Odile Sainte Catherine, Corinne Illoul, Clement Journe, Martine Jandrot-perrus, T. Coradin, Véronique Gigoux, Erwann GuéninAbstract:Fibrosis is characterized by a pathologic deposition of collagen I, leading to impaired function of organs. Tissue biopsy is the gold standard method for the diagnosis of fibrosis but this is an invasive procedure, subject to sampling errors. Several non-invasive techniques such as magnetic resonance imaging (MRI) using non-specific probes have been developed but they are not fully satisfying as they allow diagnosis at a late stage. In this study, collagelin, a collagen-Binding Peptide has been covalently linked using click chemistry to pegylated Ultra Small Super Paramagnetic Iron Oxide Nanoparticles (USPIO–PO–PEG–collagelin NPs) with the aim of diagnosing fibrosis at an early stage by MRI. USPIO–PO–PEG–collagelin NPs showed a high affinity for collagen I, two times higher than that of free collagelin whereas not Peptide labeled USPIO NPs (USPIO–PO–PEG-yne) did not present any affinity. NPs were not toxic for macrophages and fibroblasts. Diffusion through collagen hydrogels concentrated at 3 and 10 mg mL−1 revealed a large accumulation of USPIO–PO–PEG–collagelin NPs within the collagen network after 72 hours, ca. 3 times larger than that of unlabeled USPIO, thereby evidencing the specific targeting of collagen I. Moreover, the quantity of USPIO–PO–PEG–collagelin NPs accumulated within hydrogels was proportional to the collagen concentration. Subsequently, the NPs diffusion through collagen hydrogels was monitored by MRI. The MRI T2 time relaxation decreased much more significantly with depth for USPIO–PO–PEG–collagelin NPs compared to unlabeled ones. Taken together, these results show that USPIO–PEG–collagelin NPs are promising as effective MRI nanotracers for molecular imaging of fibrosis at an early stage.