
ATP는 단백질의 구조적 유연성을 조절함으로써 단백질 응집을 방지하고 용해도를 향상시킨다.


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Proteins occurring in significantly high concentrations in cellular environments (over 100 mg/mL) and functioning in crowded cytoplasm, often face the prodigious challenges of aggregation which are the pathological hallmark of aging and are critically responsible for a wide spectrum of rising human diseases. Here we combine a joint-venture of complementary wet-lab experiment and molecular simulation to discern the potential ability of adenosine triphosphate (ATP) as sollubilizer of protein aggregates. We show that ATP prevents both condensation of aggregation-prone intrinsically disordered protein Aβ40 and promotes dissolution of pre-formed aggregates. Computer simulation links ATP’s sollubilizing role to its ability to modulate protein’s structural plasticity by unwinding protein conformation. We show that ATP is positioned as a superior biological solubilizer of protein aggregates over traditional chemical hydrotropes, potentially holding promises in therapeutic interventions in protein-aggregation related diseases. Going beyond its conventional activity as energy currency, the amphiphilic nature of ATP enables its protein-specific interaction that would enhance ATP’s efficiency in cellular processes.

### Competing Interest Statement

The authors have declared no competing interest.

Elucidating ATP’s Role as Solubilizer of Biomolecular Aggregate

atp가-단백질-응집을-방지하고-단백질-용해도를-향상시키는-메커니즘


ATP가 단백질 응집을 방지하고 단백질 용해도를 향상시키는 메커니즘


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단백질 구조와 기능의 관계를 이해하기 위해 단백질 구조의 동적 특성과 화학적 특성을 반영하는 의미론적 데이터 증강 기술 NaNa와 MiGu를 제안하였으며, 이를 통해 기존 모델의 단백질 분류 성능을 크게 향상시켰다.


단백질-분류-향상을-위한-의미론적-데이터-증강-기술-nana와-migu


단백질 분류 향상을 위한 의미론적 데이터 증강 기술: NaNa와 MiGu
