지원사업
학술연구/단체지원/교육 등 연구자 활동을 지속하도록 DBpia가 지원하고 있어요.
커뮤니티
연구자들이 자신의 연구와 전문성을 널리 알리고, 새로운 협력의 기회를 만들 수 있는 네트워킹 공간이에요.
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초록· 키워드
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Objectives: Transthyretin (TTR) is a secreted homotetrameric protein that transports thyroid hormones and retinol. The absence of these bound ligands destabilizes the quaternary structure, leading to monomer formation and subsequent amyloid fibril deposition under specific conditions. Monomeric TTR, with its β-sheet-rich structure, readily forms intermolecular interactions and amyloid fibrils. Critically, extracellular TTR amyloid fibril accumulation results in transthyretin amyloidosis (ATTR). To address this pathology, stabilizing the TTR tetramer has shown promise as a therapeutic strategy. Multiple TTR stabilizers, including tafamidis, have been investigated. Tafamidis, marketed under the brand names Vandaqel and Vindamax, is currently used to treat ATTR.
Methods: In this study, we explored the binding properties of a novel indole compound, compound H, to TTR using in silico simulations and biochemical assays.
Results: We demonstrated that compound H binds to the same TTR binding site as tafamidis with superior affinity.
Conclusion: Our findings suggest that compound H has the potential to stabilize TTR tetramer and prevent amyloidogenesis. This novel compound expands the chemical space of potential TTR stabilizers, offering new avenues for the development of effective therapies for ATTR.
Methods: In this study, we explored the binding properties of a novel indole compound, compound H, to TTR using in silico simulations and biochemical assays.
Results: We demonstrated that compound H binds to the same TTR binding site as tafamidis with superior affinity.
Conclusion: Our findings suggest that compound H has the potential to stabilize TTR tetramer and prevent amyloidogenesis. This novel compound expands the chemical space of potential TTR stabilizers, offering new avenues for the development of effective therapies for ATTR.
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ABSTRACT
INTRODUCTION
MATERIALS AND METHODS
RESULTS
DISCUSSION
REFERENCES
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