scholarly journals Site-specific targeting of antibody activity in vivo mediated by disease-associated proteases

2012 ◽  
Vol 161 (3) ◽  
pp. 804-812 ◽  
Author(s):  
Oran Erster ◽  
Jerry M. Thomas ◽  
Juliana Hamzah ◽  
Abeer M. Jabaiah ◽  
Jennifer A. Getz ◽  
...  
Keyword(s):  
Antibody Activity ◽  
Site Specific ◽  
Specific Targeting

Site Specific Incorporation of Amino Acid Analogues into Proteins In Vivo

2000 ◽  
Author(s):  
Anne K. Kowal ◽  
Caroline Kohrer ◽  
Uttam L. RajBhandary
Keyword(s):  
Amino Acid ◽  
Site Specific ◽  
Amino Acid Analogues

scholarly journals Site-Specific Dual-Labeling of a VHH with a Chelator and a Photosensitizer for Nuclear Imaging and Targeted Photodynamic Therapy of EGFR-Positive Tumors

Cancers ◽  
2021 ◽  
Vol 13 (3) ◽  
pp. 428
Author(s):  
Emma Renard ◽  
Estel Collado Camps ◽  
Coline Canovas ◽  
Annemarie Kip ◽  
Martin Gotthardt ◽  
...  
Keyword(s):  
Photodynamic Therapy ◽  
Fluorescence Imaging ◽  
Ex Vivo ◽  
Growth Factor Receptor ◽  
Nuclear Imaging ◽  
A431 Cells ◽  
Site Specific ◽  
Variable Domains ◽  
Diagnostic Probe

Variable domains of heavy chain only antibodies (VHHs) are valuable agents for application in tumor theranostics upon conjugation to both a diagnostic probe and a therapeutic compound. Here, we optimized site-specific conjugation of the chelator DTPA and the photosensitizer IRDye700DX to anti-epidermal growth factor receptor (EGFR) VHH 7D12, for applications in nuclear imaging and photodynamic therapy. 7D12 was site-specifically equipped with bimodal probe DTPA-tetrazine-IRDye700DX using the dichlorotetrazine conjugation platform. Binding, internalization and light-induced toxicity of DTPA-IRDye700DX-7D12 were determined using EGFR-overexpressing A431 cells. Finally, ex vivo biodistribution of DTPA-IRDye700DX-7D12 in A431 tumor-bearing mice was performed, and tumor homing was visualized with SPECT and fluorescence imaging. DTPA-IRDye700DX-7D12 was retrieved with a protein recovery of 43%, and a degree of labeling of 0.56. Spectral properties of the IRDye700DX were retained upon conjugation. 111In-labeled DTPA-IRDye700DX-7D12 bound specifically to A431 cells, and they were effectively killed upon illumination. DTPA-IRDye700DX-7D12 homed to A431 xenografts in vivo, and this could be visualized with both SPECT and fluorescence imaging. In conclusion, the dichlorotetrazine platform offers a feasible method for site-specific dual-labeling of VHH 7D12, retaining binding affinity and therapeutic efficacy. The flexibility of the described approach makes it easy to vary the nature of the probes for other combinations of diagnostic and therapeutic compounds.

scholarly journals Xer-mediated site-specific recombination at cer generates Holliday junctions in vivo.

1994 ◽  
Vol 13 (8) ◽  
pp. 1844-1855 ◽  
Author(s):  
R. McCulloch ◽  
L.W. Coggins ◽  
S.D. Colloms ◽  
D.J. Sherratt
Keyword(s):  
Holliday Junctions ◽  
Site Specific ◽  
Site Specific Recombination

scholarly journals Peptide-tags for site-specific protein labelling in vitro and in vivo

2016 ◽  
Vol 12 (6) ◽  
pp. 1731-1745 ◽  
Author(s):  
Jonathan Lotze ◽  
Ulrike Reinhardt ◽  
Oliver Seitz ◽  
Annette G. Beck-Sickinger
Keyword(s):  
Metal Ions ◽  
Small Molecules ◽  
Protein Localization ◽  
Specific Protein ◽  
Site Specific ◽  
Protein Labelling ◽  
Peptide Interactions ◽  
Peptide Tags

Peptide-tag based labelling can be achieved by (i) enzymes (ii) recognition of metal ions or small molecules and (iii) peptide–peptide interactions and enables site-specific protein visualization to investigate protein localization and trafficking.

A Method for the Quantitative Site-Specific Study of the Biochemistry within Dental Plaque Biofilms Formed in vivo

1997 ◽  
Vol 31 (3) ◽  
pp. 194-200 ◽  
Author(s):  
C. Robinson ◽  
J. Kirkham ◽  
R. Percival ◽  
R.C. Shore ◽  
W.A. Bonass ◽  
...  
Keyword(s):  
Dental Plaque ◽  
Site Specific ◽  
Specific Study

scholarly journals Variations in the Botulinum Neurotoxin Binding Domain and the Potential for Novel Therapeutics

Toxins ◽  
2018 ◽  
Vol 10 (10) ◽  
pp. 421 ◽  
Author(s):  
Jonathan Davies ◽  
Sai Liu ◽  
K. Acharya
Keyword(s):  
Botulinum Neurotoxin ◽  
Neuronal Cell ◽  
Binding Domain ◽  
Novel Therapeutics ◽  
Specific Targeting ◽  
Zinc Metalloprotease ◽  
Botulinum Neurotoxins ◽  
Translocation Domain ◽  
Subtype Differences

Botulinum neurotoxins (BoNTs) are categorised into immunologically distinct serotypes BoNT/A to /G). Each serotype can also be further divided into subtypes based on differences in amino acid sequence. BoNTs are ~150 kDa proteins comprised of three major functional domains: an N-terminal zinc metalloprotease light chain (LC), a translocation domain (HN), and a binding domain (HC). The HC is responsible for targeting the BoNT to the neuronal cell membrane, and each serotype has evolved to bind via different mechanisms to different target receptors. Most structural characterisations to date have focussed on the first identified subtype within each serotype (e.g., BoNT/A1). Subtype differences within BoNT serotypes can affect intoxication, displaying different botulism symptoms in vivo, and less emphasis has been placed on investigating these variants. This review outlines the receptors for each BoNT serotype and describes the basis for the highly specific targeting of neuronal cell membranes. Understanding receptor binding is of vital importance, not only for the generation of novel therapeutics but also for understanding how best to protect from intoxication.

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