Embark on a nautical expedition through five key molecular interactions of neurotoxin α-conotoxin-ImI and its inhibition of Ac-AChBP, with a sea-themed narrative. Isolated from the venom of cone snail Conus imperialis, the amino acid sequence of cyclic peptide α-conotoxin-ImI exhibits a unique closed ring structure, granting high affinity and selectivity for protein targets, large surface area, and resistance to enzymatic degradation. α-conotoxin ImI inhibits nicotinic acetylcholine receptors (nAchRs) at neuromuscular junctions, notably Ac-AchBP, a homolog of the ligand binding domain of nAchR found in Aplysia californica. Ride the waves of scientific discovery as α-conotoxin ImI emerges as a possible therapeutic drug candidate to treat chronic pain by its unique specificity and calcium channel activity in neurotransmitters.
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