scholarly journals Development and activities, including immunocomplex formation, of biparatopic antibodies and alternative scaffold proteins

2020 ◽  
Vol 2 (1) ◽  
pp. 1-6
Author(s):  
Hiroki AKIBA ◽  
Kouhei TSUMOTO
2011 ◽  
Vol 37 (5) ◽  
pp. 517-526 ◽  
Author(s):  
L. E. Petrovskaya ◽  
L. N. Shingarova ◽  
D. A. Dolgikh ◽  
M. P. Kirpichnikov

2018 ◽  
Vol 8 (6) ◽  
pp. 930 ◽  
Author(s):  
Diana Zárate-Triviño ◽  
Sara Hernández-Martínez ◽  
Juan Bollain-y-Goytia-de-la-Rosa ◽  
Moisés Franco-Molina ◽  
Eduardo Elizalde-Peña ◽  
...  

2021 ◽  
Vol 4 (1) ◽  
Author(s):  
Niels Wicke ◽  
Mike R. Bedford ◽  
Mark Howarth

AbstractProtein-based targeting reagents, such as antibodies and non-antibody scaffold proteins, are rapidly inactivated in the upper gastrointestinal (GI) tract. Hydrochloric acid in gastric juice denatures proteins and activates pepsin, concentrations of which reach 1 mg/mL in the mammalian stomach. Two stable scaffold proteins (nanobody and nanofitin), previously developed to be protease-resistant, were completely digested in less than 10 min at 100-fold lower concentration of pepsin than found in the stomach. Here we present gastrobodies, a protein scaffold derived from Kunitz soybean trypsin inhibitor (SBTI). SBTI is highly resistant to the challenges of the upper GI tract, including digestive proteases, pH 2 and bile acids. Computational prediction of SBTI’s evolvability identified two nearby loops for randomization, to create a potential recognition surface which was experimentally validated by alanine scanning. We established display of SBTI on full-length pIII of M13 phage. Phage selection of gastrobody libraries against the glucosyltransferase domain of Clostridium difficile toxin B (GTD) identified hits with nanomolar affinity and enzyme inhibitory activity. Anti-GTD binders retained high stability to acid, digestive proteases and heat. Gastrobodies show resilience to exceptionally harsh conditions, which should provide a foundation for targeting and modulating function within the GI tract.


2014 ◽  
Vol 106 (2) ◽  
pp. 476a
Author(s):  
James McCann ◽  
Ucheor B. Choi ◽  
Mark E. Bowen
Keyword(s):  

2005 ◽  
Vol 135 (1-2) ◽  
pp. 204-216 ◽  
Author(s):  
Zhang Jing-Ping ◽  
Qing-Bao Tian ◽  
Hiroyuki Sakagami ◽  
Hisatake Kondo ◽  
Shogo Endo ◽  
...  
Keyword(s):  

2019 ◽  
Vol 16 (2) ◽  
pp. 183-189
Author(s):  
Y. M. Nemesh ◽  
S. V. Kropyvko

Aim. TKS5 is a key scaffold protein of invadopodia. In its absence, the cells completely lose the ability to form invadopodia. This fact makes TKS5 a potential target for cancer cure and one of the central proteins in the investigation of cancer cell invasion. Additionally, the question remains about the function of TKS5 in normal cells. Therefore, in order to extend knowledge about TKS5 role in healthy and invasive cells, we tested the TKS5 interaction with the proteins involved in signal transduction: PLCγ1, SRC, CRK, CSK; the proteins involved in plasma membrane remodeling: AMPH1, BIN1, CIN85, ITSN1, ITSN2; the protein involved in the actin cytoskeleton rearrangement: CTTN. Methods. We used the GST Pull-down assay to identify the protein-protein interaction. Results. We revealed that TKS5 SH3 domains interact with CIN85. There were identified TKS5 interactions with SH3 domains of CTTN, ITSN1, ITSN2, AMPH1 and BIN1. Conclusions. TKS5 interacts with CIN85, CTTN, ITSN1, ITSN2, AMPH1 and BIN1, which take part in membrane remodeling, endo-/exocytosis and actin cytoskeleton rearrangement. Keywords: TKS5, scaffold proteins, actin cytoskeleton, plasma membrane.


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