Site-Specific Labeling of Proteins with a Chemically Stable, High-Affinity Tag for Protein Study

2012 ◽  
Vol 19 (3) ◽  
pp. 1097-1103 ◽  
Author(s):  
Yin Yang ◽  
Qing-Feng Li ◽  
Chan Cao ◽  
Feng Huang ◽  
Xun-Cheng Su
Keyword(s):  
Affinity Tag ◽  
Site Specific ◽  
High Affinity

Site-Specific Quantification of Persulfidome by Combining an Isotope-Coded Affinity Tag with Strong Cation-Exchange-Based Fractionation

2019 ◽  
Vol 91 (23) ◽  
pp. 14860-14864 ◽  
Author(s):  
Qiong Wu ◽  
Baofeng Zhao ◽  
Yejing Weng ◽  
Yichu Shan ◽  
Xiao Li ◽  
...  
Keyword(s):  
Cation Exchange ◽  
Affinity Tag ◽  
Site Specific ◽  
Strong Cation Exchange

Design of Coordination Interaction of Zn(II) Complex with Oligo-Aspartate Peptide to Afford a High-Affinity Tag–Probe Pair

2015 ◽  
Vol 88 (6) ◽  
pp. 784-791 ◽  
Author(s):  
Hirokazu Fuchida ◽  
Shigekazu Tabata ◽  
Naoya Shindo ◽  
Ippei Takashima ◽  
Qiao Leng ◽  
...  
Keyword(s):  
Probe Pair ◽  
Coordination Interaction ◽  
Affinity Tag ◽  
High Affinity

scholarly journals ‘Traceless’ tracing of proteins – high-affinity trans-splicing directed by a minimal interaction pair

2016 ◽  
Vol 7 (4) ◽  
pp. 2646-2652 ◽  
Author(s):  
M. Braner ◽  
A. Kollmannsperger ◽  
R. Wieneke ◽  
R. Tampé
Keyword(s):  
Mammalian Cells ◽  
Protein Labeling ◽  
Terminal Protein ◽  
Site Specific ◽  
High Affinity ◽  
Trans Splicing

Using a minimal lock-and-key element the affinity between the intein fragments for N-terminal protein trans-splicing was significantly increased, allowing for site-specific, ‘traceless’ covalent protein labeling in living mammalian cells at nanomolar probe concentrations.

ChemInform Abstract: Design of Coordination Interaction of Zn(II) Complex with Oligo-Aspartate Peptide to Afford a High-Affinity Tag-Probe Pair.

ChemInform ◽  
2015 ◽  
Vol 46 (36) ◽  
pp. no-no
Author(s):  
Hirokazu Fuchida ◽  
Shigekazu Tabata ◽  
Naoya Shindo ◽  
Ippei Takashima ◽  
Qiao Leng ◽  
...  
Keyword(s):  
Probe Pair ◽  
Coordination Interaction ◽  
Affinity Tag ◽  
High Affinity

scholarly journals Current Strategies for Microbubble-Based Thrombus Targeting: Activation-Specific Epitopes and Small Molecular Ligands

2021 ◽  
Vol 9 ◽  
Author(s):  
Zhaojian Wang ◽  
Huaigu Huang ◽  
Yuexin Chen ◽  
Yuehong Zheng
Keyword(s):  
Free Drug ◽  
Site Specific ◽  
High Affinity ◽  
Activated Platelets ◽  
Thrombotic Diseases ◽  
Carrier Systems

Microbubbles with enhanced ultrasound represent a potentially potent evolution to the administration of a free drug in the treatment of thrombotic diseases. Conformational and expressional changes of several thrombotic biological components during active coagulation provide epitopes that allow site-specific delivery of microbubble-based agents to the thrombus for theranostic purpose. Through the interaction with these epitopes, emerging high-affinity small molecular ligands are able to selectively target the thrombi with tremendous advantages over traditional antibody-based strategy. In this mini-review, we summarize recent novel strategies for microbubble-based targeting of thrombus through epitopes located at activated platelets and fibrin. We also discuss the challenges of current targeting modalities and supramolecular carrier systems for their translational use in thrombotic pathologies.

Role of calmodulin methionine residues in mediating productive association with cardiac ryanodine receptors

2006 ◽  
Vol 290 (2) ◽  
pp. H794-H799 ◽  
Author(s):  
Edward M. Balog ◽  
Laura E. Norton ◽  
David D. Thomas ◽  
Bradley R. Fruen
Keyword(s):  
Sarcoplasmic Reticulum ◽  
Cardiac Muscle ◽  
Ryanodine Receptor ◽  
Ryanodine Receptors ◽  
Release Channel ◽  
Site Specific ◽  
High Affinity ◽  
Methionine Residues ◽  
Cardiac Ryanodine Receptor

Calmodulin (CaM) binds to the cardiac ryanodine receptor Ca2+ release channel (RyR2) with high affinity and may act as a regulatory channel subunit. Here we determine the role of CaM Met residues in the productive association of CaM with RyR2, as assessed via determinations of [3H]ryanodine and [35S]CaM binding to cardiac muscle sarcoplasmic reticulum (SR) vesicles. Oxidation of all nine CaM Met residues abolished the productive association of CaM with RyR2. Substitution of the COOH-terminal Mets of CaM with Leu decreased the extent of CaM inhibition of cardiac SR (CSR) vesicle [3H]ryanodine binding. In contrast, replacing the NH2-terminal Met of CaM with Leu increased the concentration of CaM required to inhibit CSR [3H]ryanodine binding but did not alter the extent of inhibition. Site-specific substitution of individual CaM Met residues with Gln demonstrated that Met124 was required for both high-affinity CaM binding to RyR2 and for maximal CaM inhibition. These results thus identify a Met residue critical for the productive association of CaM with RyR2 channels.

Development of a high‐affinity antibody‐binding peptide for site‐specific modification

ChemMedChem ◽  
2021 ◽  
Author(s):  
Kyohei Muguruma ◽  
Rento Osawa ◽  
Akane Fukuda ◽  
Naoto Ishikawa ◽  
Konomi Fujita ◽  
...  
Keyword(s):  
Antibody Binding ◽  
Site Specific ◽  
Binding Peptide ◽  
Specific Modification ◽  
High Affinity
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