Qualitative and Quantitative Proteomic Analysis of Venoms from Mexican Rattlesnakes

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  Qualitative and Quantitative Proteomic Analysis of Venoms from Mexican Rattlesnakes Abstract Despite the vast biodiversity of Mexican vipers, venom of endemic species has been barely studied. Here we analyzed the venom composition of three endemic species of rattlesnakes: Crotalus aquilus , C. triseriatus , and C. ravus . We used quantitative chromato-mass-spectrometry and compared venoms with C. molossus , a species commonly found in North America, in a comparative and phylogenetic framework. In total, we identified 165 proteins grouped in 19 main protein families, consistent with previous reports for viperid venoms. In C. aquilus and C. triseriatus , the most predominant protein-family type was Serine Proteases, and in C. triseriatus and C. molossus it was Snake Venom Metalloproteases. The Label-free quantification revealed a high proportion of Snake Venom Metalloproteases in C. aquilus , C. triseriatus , and C. molossus , reaching 28–47% of the total venom. In contrast, in ...

Exploring Venom-derived Peptides from Calloselasma rhodostoma Snake as Promising Cholinesterase Inhibitors for Alzheimer’s Disease Therapy

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By Wibowo Djatmiko (Wie146) - Own work, CC BY-SA 3.0, https://commons.wikimedia.org/w/index.php?curid=21623901

Exploring Venom-derived Peptides from Calloselasma rhodostoma Snake as Promising Cholinesterase Inhibitors for Alzheimer’s Disease Therapy

Alzheimer’s disease (AD) is a neurodegenerative disorder that primarily affects individuals over 60 years of age, characterized by symptoms such as memory impairment and cognitive decline. The pathogenesis of AD involves multiple factors, including protein misfolding and oxidative stress. A crucial aspect of AD progression is the dysregulation of cholinesterase enzymes, particularly acetylcholinesterase (AChE) and butyrylcholinesterase (BChE), which contribute to neurotoxic amyloid plaques and neurofibrillary tangles. This study investigates the potential of proteins and peptides from the venom of Calloselasma rhodostoma as BChE inhibitors, aiming to explore new therapeutic avenues for AD. Venom was extracted, fractionated, and analyzed using ultrafiltration, SDS-PAGE, and LC-HRMS. In vitro assays evaluated the BChE inhibition activity, while in silico molecular docking assessed the binding affinities of the identified peptides. The study identified several venom-derived peptides with significant BChE inhibitory potential, notably CFVVQPWEGK and IDVLSDEPR, which demonstrated strong binding affinities and stability in docking studies. These findings highlight the potential of peptides derived from C. rhodostoma venom as natural BChE inhibitors, offering a promising basis for developing novel AD therapies. Further research is warranted to fully understand the mechanisms and therapeutic potential of these bioactive compounds.

Exploring Venom-derived Peptides from Calloselasma rhodostoma Snake as Promising Cholinesterase Inhibitors for Alzheimer’s Disease Therapy

Annisa Maghfira, Itsar Auliya, Tri Rini Nuringtyas, Fajar Sofyantoro, Donan Satria Yudha, Slamet Raharjo, and Yekti Asih Purwestri