Fluorescence study for selecting specific ligands toward HER2 receptor: An example of receptor fragment approach

Calce, Enrica; Monfregola, Luca; Sandomenico, Annamaria; Luca, Stefania De

doi:10.1016/j.ejmech.2012.09.024

Cited by 17 publications

(17 citation statements)

References 31 publications

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“…Fluorescence spectrum could reflect the information of tyrosine ( Tyr ) and tryptophan ( Trp ) when the excitation wavelength was set as 280 nm (Calce et al, 2013). Figure 2A showed the fluorescence quenching of BSA with 5-CQA, and that of BSA with 3-CQA and 4-CQA was shown in Supplementary Figure 1.…”

Section: Resultsmentioning

confidence: 99%

Study on the Interactions Between Caffeoylquinic Acids With Bovine Serum Albumin: Spectroscopy, Antioxidant Activity, LC-MSn, and Molecular Docking Approach

et al. 2019

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Clarified the binding mechanism of drugs with plasma proteins could provide fresh insights into the drug development. Caffeoylquinic acids (CQAs) are a kind of phenolic acid compounds which has extensive biological effects. This study investigated the binding mechanism of three CQAs, including chlorogenic acid, neochlorogenic acid, and cryptochlorogenic acid, with bovine serum albumin (BSA) by using multi-spectroscopic techniques, including fluorescence, UV-Vis, Fourier transform infrared (FT-IR) and circular dichroism (CD) spectroscopy, LC-MSn, molecular docking and antioxidant activity assessment. In addition, the influences of PBS buffer, Tris-HCl buffer and water as solvents on the characteristics of CQAs and BSA interaction were also investigated. The results showed that intrinsic fluorescence of BSA was quenched by CQAs and the interaction was static quenching with the formation of a non-fluorescent complex. The binding of CQAs and BSA was spontaneous, and Van der Waals forces and hydrogen-bond interaction occupied crucial roles in the binding. All the three CQAs could bind to Site I in Domain IIA. The weakest interaction between neochlorogenic acid and BSA may due to its larger polarity. The results also indicated that the binding affinity of CQAs had a descending order of Tris-HCl > H2O > PBS. This study firstly clarified the binding mechanism of CQAs with BSA and changes of the binding in different solvents, and provided fresh insights into this drug transportation and metabolism.

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Section: Resultsmentioning

confidence: 99%

Study on the Interactions Between Caffeoylquinic Acids With Bovine Serum Albumin: Spectroscopy, Antioxidant Activity, LC-MSn, and Molecular Docking Approach

et al. 2019

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“…As we have already done in a previous study, we adopted the receptor fragment approach in order to investigate the interaction process between the A9-dimer and HER2-DIVMP (Calce et al 2013).…”

Section: Fluorescence Studiesmentioning

confidence: 99%

“…On the basis of these considerations, we have selected several peptides (A9, A12 and B12) from the Herceptin Fab region in contact with HER2 ECD, in order to study these new molecules as potential ligands specific for the receptor target (Calce et al 2013). In particular, A9 and A12 were derived from the antibody heavy chain, while B12 from its light chain.…”

Section: Introductionmentioning

confidence: 99%

“…In particular, since the peptide A9 revealed to have the highest affinity to the receptor model (Calce et al 2013), we hypothesized its potential use for targeted delivery of chemotherapeutic or imaging agents to HER2-expressing tumor cells. In this regard, a further enhancement and optimization of the receptor binding affinity could improve tumor targeting of the peptide.…”

Section: Introductionmentioning

confidence: 99%

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Development of Targeting Ligands for HER2 Receptor: Simplified Receptor Model Employed for Selecting Highly Specific Molecules

Calce

Luca

2015

Int J Pept Res Ther

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The interaction between Herceptin (Fab)-derived dimeric peptide and HER2-DIVMP, a synthetic peptide mimicking the subdomain IV of the receptor HER2, was monitored by fluorescence spectroscopy method. The obtained results confirmed that the adopted mimetic receptor fragment represents a reliable model system to monitor the ability of selected ligands to bind the receptor target, avoiding the involvement of cells or cellular extracts in a preliminary binding assay. Moreover, HER2-DIVMP has the characteristics of being easily integrated in rapid, efficient and inexpensive screening method for optimizing small molecules as targeting ligands for the receptor-mediated anticancer therapy.

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“…In this context, we have recently developed and studied several trastuzumab (Fab)-derived peptides capable to bind HER2 41 . In particular, the A9 peptide was found to be particularly interesting, since it showed a dissociation constant in nanomolar range for the receptor model HER2-DIVMP 41 – 43 . Therefore, it was studied as a promising candidate for development of an HER2-specific imaging probe.…”

Section: Introductionmentioning

confidence: 99%

Evaluation of HER2-specific peptide ligand for its employment as radiolabeled imaging probe

Honarvar

Calce

Doti

et al. 2018

Sci Rep

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HER2 transmembrane receptor is an important target in immunotherapy treatment of breast and gastroesophageal cancer. Molecular imaging of HER2 expression may provide essential prognostic and predictive information concerning disseminated cancer and aid in selection of an optimal therapy. Radiolabeled low molecular weight peptide ligands are particularly attractive as probes for molecular imaging, since they reach and bind to the target and clear from non-target organs and blood stream faster than bulky antibodies. In this study, we evaluated a potential HER2-imaging probe, an A9 nonapeptide, derived from the trastuzumab-Fab portion. Its cellular uptake was investigated by mass spectrometry analysis of the cytoplasmic cellular extracts. Moreover, based on in-silico modeling, DTPA chelator was conjugated to N-terminus of A9. 111In-labeled A9 demonstrated nanomolar affinity to HER2-expressing BT474 cells and favorable biodistribution profile in NMRI mice. This study suggests that the peptide A9 represents a good lead candidate for development of molecular probe, to be used for imaging purposes and for the delivery of cytotoxic agents.

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Fluorescence study for selecting specific ligands toward HER2 receptor: An example of receptor fragment approach

Cited by 17 publications

References 31 publications

Study on the Interactions Between Caffeoylquinic Acids With Bovine Serum Albumin: Spectroscopy, Antioxidant Activity, LC-MSn, and Molecular Docking Approach

Study on the Interactions Between Caffeoylquinic Acids With Bovine Serum Albumin: Spectroscopy, Antioxidant Activity, LC-MSn, and Molecular Docking Approach

Development of Targeting Ligands for HER2 Receptor: Simplified Receptor Model Employed for Selecting Highly Specific Molecules

Evaluation of HER2-specific peptide ligand for its employment as radiolabeled imaging probe

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