FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W3092051218> ?p ?o ?g. }

• W3092051218 abstract "Snakebite envenomations has for a long time been an overlooked problem, despite the hundreds of thousands of deaths and disabilities caused by this disease each year. However, since snakebite envenoming predominantly affects the rural areas of third-world countries, there was an absence of research funding and drive to address this profound concern. Consequently, costly and often highly immunogenic animal-derived antivenoms still constitute the sole treatment option for snakebite envenomations.Fortunately, public interest and funding has increased in the last decade, thereby, presenting a new horizon for snakebite therapeutics. This has led to a shift in how researchers approach the treatment of envenomations. It has been proposed that, instead of targeting the whole venom, one could focus on only neutralising the clinically relevant toxins within the venom. Moreover, the advancement in antibody research has led to novel approaches towards treating snakebite envenomings, such as the utilization of human monoclonal immunoglobulin G antibodies (IgGs). Whilst IgGs present a thoroughly investigated and highly reliable therapeutic scaffold, its rather large size (150 kDa) could present hurdles in neutralizing certain toxins quickly (especially in deep tissue) and the associated manufacturing costs could also complicate its global deployment to the poorer regions of the globe. Small non-antibody-scaffolds present a promising alternative, since they are likely to overcome some of the key limitations of IgGs, while retaining most of their benefits. Particularly, designed ankyrin repeat proteins (DARPins) carry significant promise due to their impressive safety profile in humans, high thermostability, low manufacturing cost, and high engineerability. Therefore, this thesis aimed to establish the capability of DARPins to bind with high-affinity to α-cobratoxin from monocled Cobra (Naja Kaouthia). To achieve this, the power of the phage display technique was harnessed to screen a DARPin-library to discover α-cobratoxin-specific binders. Following four panning rounds, the outputs were evaluated via plate tests and polyclonal ELISAs. Unfortunately, numerous issues arose throughout this thesis, complicating and slowing down the selection process. In the end, no α-cobratoxin-specific DARPin binders were discovered and there was no time to repeat the selection process. Nevertheless, key issues have been identified and solutions have been proposed to ensure that future selection campaigns will hopefully be efficient and successful. Indeed, whilst antibody discovery can be complicated, time-consuming, and often relies on a certain amount of luck, I have no doubt that my first steps towards a first-ever snake toxin binding DARPin will aid in the endeavour of harnessing the potential of this scaffold in the context of next-generation antivenoms. Hopefully, this will eventually lead to a substantial improvement in the treatment of snakebite evenomations and help alleviate the global health burden that is snakebite." @default.
• W3092051218 created "2020-10-15" @default.
• W3092051218 creator A5011899341 @default.
• W3092051218 date "2020-01-01" @default.
• W3092051218 modified "2023-09-27" @default.
• W3092051218 title "Discovery of a DARPin-based antitoxin against α-cobratoxin" @default.
• W3092051218 hasPublicationYear "2020" @default.
• W3092051218 type Work @default.
• W3092051218 sameAs 3092051218 @default.
• W3092051218 citedByCount "0" @default.
• W3092051218 crossrefType "journal-article" @default.
• W3092051218 hasAuthorship W3092051218A5011899341 @default.
• W3092051218 hasConcept C144133560 @default.
• W3092051218 hasConcept C145600735 @default.
• W3092051218 hasConcept C177713679 @default.
• W3092051218 hasConcept C18903297 @default.
• W3092051218 hasConcept C203014093 @default.
• W3092051218 hasConcept C2777367657 @default.
• W3092051218 hasConcept C2778973234 @default.
• W3092051218 hasConcept C2779448229 @default.
• W3092051218 hasConcept C71924100 @default.
• W3092051218 hasConcept C86803240 @default.
• W3092051218 hasConcept C89423630 @default.
• W3092051218 hasConceptScore W3092051218C144133560 @default.
• W3092051218 hasConceptScore W3092051218C145600735 @default.
• W3092051218 hasConceptScore W3092051218C177713679 @default.
• W3092051218 hasConceptScore W3092051218C18903297 @default.
• W3092051218 hasConceptScore W3092051218C203014093 @default.
• W3092051218 hasConceptScore W3092051218C2777367657 @default.
• W3092051218 hasConceptScore W3092051218C2778973234 @default.
• W3092051218 hasConceptScore W3092051218C2779448229 @default.
• W3092051218 hasConceptScore W3092051218C71924100 @default.
• W3092051218 hasConceptScore W3092051218C86803240 @default.
• W3092051218 hasConceptScore W3092051218C89423630 @default.
• W3092051218 hasLocation W30920512181 @default.
• W3092051218 hasOpenAccess W3092051218 @default.
• W3092051218 hasPrimaryLocation W30920512181 @default.
• W3092051218 hasRelatedWork W116895358 @default.
• W3092051218 hasRelatedWork W2070366844 @default.
• W3092051218 hasRelatedWork W2887069993 @default.
• W3092051218 isParatext "false" @default.
• W3092051218 isRetracted "false" @default.
• W3092051218 magId "3092051218" @default.
• W3092051218 workType "article" @default.