Elucidating ATP’s role as solubilizer of biomolecular aggregate DOI Creative Commons

Susmita Sarkar,

Saurabh Gupta,

Chiranjit Mahato

и другие.

eLife, Год журнала: 2024, Номер 13

Опубликована: Окт. 30, 2024

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

Язык: Английский

Elucidating ATP’s Role as Solubilizer of Biomolecular Aggregate DOI Creative Commons

Susmita Sarkar,

Saurabh Gupta,

Chiranjit Mahato

и другие.

eLife, Год журнала: 2024, Номер 13

Опубликована: Июль 10, 2024

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

Язык: Английский

Процитировано

3
Elucidating ATP’s Role as Solubilizer of Biomolecular Aggregate DOI Open Access

Susmita Sarkar,

Saurabh Gupta,

Chiranjit Mahato

и другие.

Опубликована: Сен. 24, 2024

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

Язык: Английский

Процитировано

3
Elucidating ATP’s Role as Solubilizer of Biomolecular Aggregate DOI Creative Commons

Susmita Sarkar,

Saurabh Gupta,

Chiranjit Mahato

и другие.

bioRxiv (Cold Spring Harbor Laboratory), Год журнала: 2024, Номер unknown

Опубликована: Янв. 16, 2024

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

Язык: Английский

Процитировано

1
Elucidating ATP’s role as solubilizer of biomolecular aggregate DOI Creative Commons

Susmita Sarkar,

Saurabh Gupta,

Chiranjit Mahato

и другие.

eLife, Год журнала: 2024, Номер 13

Опубликована: Окт. 30, 2024

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

Язык: Английский

Процитировано

0