Coamorphous Lurasidone Hydrochloride–Saccharin with Charge-Assisted Hydrogen Bonding Interaction Shows Improved Physical Stability and Enhanced Dissolution with pH-Independent Solubility Behavior

2015 ◽  
Vol 15 (6) ◽  
pp. 2920-2928 ◽  
Author(s):  
Shuai Qian ◽  
Weili Heng ◽  
Yuanfeng Wei ◽  
Jianjun Zhang ◽  
Yuan Gao
Keyword(s):  
Hydrogen Bonding ◽  
Physical Stability ◽  
Hydrogen Bonding Interaction ◽  
Enhanced Dissolution ◽  
Solubility Behavior ◽  
Bonding Interaction ◽  
Lurasidone Hydrochloride

A novel lurasidone hydrochloride–shikimic acid co-amorphous system formed by hydrogen-bonding interaction with the retained pH-dependent solubility behavior

CrystEngComm ◽  
2020 ◽  
Vol 22 (35) ◽  
pp. 5841-5853
Author(s):  
Yi Hu ◽  
Cuiping Jiang ◽  
Bin Li ◽  
Lijing Zhou ◽  
Renjie Xu ◽  
...  
Keyword(s):  
Hydrogen Bonding ◽  
Organic Acid ◽  
Shikimic Acid ◽  
Hydrogen Bonding Interaction ◽  
Amorphous System ◽  
Solubility Behavior ◽  
Bonding Interaction ◽  
New Type ◽  
Ph Dependent ◽  
Lurasidone Hydrochloride

The current study was aimed at investigating the lurasidone hydrochloride–shikimic acid co-amorphous system using a new type of organic acid.

Charge-assisted intermolecular hydrogen bond formed in coamorphous system is important to relieve the pH-dependent solubility behavior of lurasidone hydrochloride

RSC Advances ◽  
2016 ◽  
Vol 6 (108) ◽  
pp. 106396-106412 ◽  
Author(s):  
Shuai Qian ◽  
Zhen Li ◽  
Weili Heng ◽  
Shujun Liang ◽  
Di Ma ◽  
...  
Keyword(s):  
Hydrogen Bond ◽  
Dissolution Rate ◽  
Intermolecular Hydrogen Bond ◽  
Physical Stability ◽  
Enhanced Dissolution ◽  
Solubility Behavior ◽  
Dependent Behavior ◽  
Ph Dependent ◽  
Lurasidone Hydrochloride

In comparison to amorphous LH, coamorphous LH-REP without evidence of intermolecular hydrogen bond, exhibited greatly improved solubility with pH-dependent behavior, significantly enhanced dissolution rate and physical stability.

Radical Enzymes Control the Chemistry of Their Highly Reactive Intermediates Using the Quantum Coulombic Effect

2020 ◽  
Author(s):  
Hossein Khalilian ◽  
Gino A. DiLabio
Keyword(s):  
Hydrogen Bonding ◽  
Molecular Orbital ◽  
Reactive Intermediates ◽  
Hydrogen Bonding Interaction ◽  
Orbital Ordering ◽  
Dynamic Nature ◽  
Radical Intermediate ◽  
Highest Occupied Molecular Orbital ◽  
Bonding Interaction ◽  
Close Proximity

Here, we report an exquisite strategy that the B12 enzymes exploit to manipulate the reactivity of their radical intermediate (Adenosyl radical). Based on the quantum-mechanic calculations, these enzymes utilize a little known long-ranged through space quantum Coulombic effect (QCE). The QCE causes the radical to acquire an electronic structure that contradicts the Aufbau Principle: The singly-occupied molecular orbital (SOMO) is no longer the highest-occupied molecular orbital (HOMO) and the radical is unable to react with neighbouring substrates. The dynamic nature of the enzyme and its structure is expected to be such that the reactivity of the radical is not restored until it is moved into close proximity of the target substrate. We found that the hydrogen bonding interaction between the nearby conserved glutamate residue and the ribose ring of Adenosyl radical plays a crucial role in manipulating the orbital ordering

Radical Enzymes Control the Chemistry of Their Highly Reactive Intermediates Using the Quantum Coulombic Effect

2020 ◽  
Author(s):  
Hossein Khalilian ◽  
Gino A. DiLabio
Keyword(s):  
Hydrogen Bonding ◽  
Molecular Orbital ◽  
Reactive Intermediates ◽  
Hydrogen Bonding Interaction ◽  
Orbital Ordering ◽  
Dynamic Nature ◽  
Radical Intermediate ◽  
Highest Occupied Molecular Orbital ◽  
Bonding Interaction ◽  
Close Proximity

Here, we report an exquisite strategy that the B12 enzymes exploit to manipulate the reactivity of their radical intermediate (Adenosyl radical). Based on the quantum-mechanic calculations, these enzymes utilize a little known long-ranged through space quantum Coulombic effect (QCE). The QCE causes the radical to acquire an electronic structure that contradicts the Aufbau Principle: The singly-occupied molecular orbital (SOMO) is no longer the highest-occupied molecular orbital (HOMO) and the radical is unable to react with neighbouring substrates. The dynamic nature of the enzyme and its structure is expected to be such that the reactivity of the radical is not restored until it is moved into close proximity of the target substrate. We found that the hydrogen bonding interaction between the nearby conserved glutamate residue and the ribose ring of Adenosyl radical plays a crucial role in manipulating the orbital ordering

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