scholarly journals Fc-fusion mimetics

2016 ◽  
Vol 4 (6) ◽  
pp. 943-947 ◽  
Author(s):  
H. Khalili ◽  
P. T. Khaw ◽  
S. Brocchini
Keyword(s):  
Disulfide Bridging

The Fc-fusion mimetic RpR 2̲ was prepared by disulfide bridging conjugation using PEG in the place of the Fc.

Chemically generated IgG2 bispecific antibodies through disulfide bridging

2017 ◽  
Vol 27 (16) ◽  
pp. 3647-3652 ◽  
Author(s):  
James T. Patterson ◽  
Edwige Gros ◽  
Heyue Zhou ◽  
Ghazi Atassi ◽  
Lisa Kerwin ◽  
...  
Keyword(s):  
Bispecific Antibodies ◽  
Disulfide Bridging

scholarly journals Self-homodimerization of an actinoporin by disulfide bridging reveals implications for their structure and pore formation

2018 ◽  
Vol 8 (1) ◽  
Author(s):  
Aisel Valle ◽  
Luis Benito Pérez-Socas ◽  
Liem Canet ◽  
Yadira de la Patria Hervis ◽  
German de Armas-Guitart ◽  
...  
Keyword(s):  
Pore Formation ◽  
Disulfide Bridging

scholarly journals Functional native disulfide bridging enables delivery of a potent, stable and targeted antibody–drug conjugate (ADC)

2015 ◽  
Vol 51 (53) ◽  
pp. 10624-10627 ◽  
Author(s):  
João P. M. Nunes ◽  
Maurício Morais ◽  
Vessela Vassileva ◽  
Eifion Robinson ◽  
Vineeth S. Rajkumar ◽  
...  
Keyword(s):  
Blood Serum ◽  
Next Generation ◽  
High Potency ◽  
Antibody Drug Conjugate ◽  
Drug Conjugate ◽  
Disulfide Bridging ◽  
Antibody Drug ◽  
Excellent Stability

A next generation maleimide–ADC is shown to have excellent stability in blood serum, as well as high potency and selectivity in vitro.

The importance of disulfide bridging

2005 ◽  
Vol 23 (1) ◽  
pp. 71-73 ◽  
Author(s):  
Harold E. Swaisgood
Keyword(s):  
Disulfide Bridging

scholarly journals C-mannosylation supports folding and enhances stability of thrombospondin repeats

eLife ◽  
2019 ◽  
Vol 8 ◽  
Author(s):  
Aleksandra Shcherbakova ◽  
Matthias Preller ◽  
Manuel H Taft ◽  
Jordi Pujols ◽  
Salvador Ventura ◽  
...  
Keyword(s):  
Significant Proportion ◽  
Experimental Studies ◽  
Intramolecular Hydrogen Bonding ◽  
Tryptophan Residues ◽  
Disulfide Bridging ◽  
Dynamics Simulations ◽  
Intramolecular Hydrogen ◽  
Thrombospondin Type 1 Repeats

Previous studies demonstrated importance of C-mannosylation for efficient protein secretion. To study its impact on protein folding and stability, we analyzed both C-mannosylated and non-C-mannosylated thrombospondin type 1 repeats (TSRs) of netrin receptor UNC-5. In absence of C-mannosylation, UNC-5 TSRs could only be obtained at low temperature and a significant proportion displayed incorrect intermolecular disulfide bridging, which was hardly observed when C-mannosylated. Glycosylated TSRs exhibited higher resistance to thermal and reductive denaturation processes, and the presence of C-mannoses promoted the oxidative folding of a reduced and denatured TSR in vitro. Molecular dynamics simulations supported the experimental studies and showed that C-mannoses can be involved in intramolecular hydrogen bonding and limit the flexibility of the TSR tryptophan-arginine ladder. We propose that in the endoplasmic reticulum folding process, C-mannoses orient the underlying tryptophan residues and facilitate the formation of the tryptophan-arginine ladder, thereby influencing the positioning of cysteines and disulfide bridging.

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