Complementary hydrogen bonding interaction triggered co-assembly of an amphiphilic peptide and an anti-tumor drug

2015 ◽  
Vol 51 (32) ◽  
pp. 6936-6939 ◽  
Author(s):  
Hong Cheng ◽  
Yin-Jia Cheng ◽  
Sushant Bhasin ◽  
Jing-Yi Zhu ◽  
Xiao-Ding Xu ◽  
...  

A new tumor-targeting amphiphilic peptide was designed to load and release the anti-tumor drug methotrexate (MTX), leading to reversible self-assembled morphology transition from spherical micelles to nanofibers.

Langmuir ◽  
2006 ◽  
Vol 22 (19) ◽  
pp. 8127-8133 ◽  
Author(s):  
Rui Li ◽  
Xinlin Yang ◽  
Guoliang Li ◽  
Shuning Li ◽  
Wenqiang Huang

2015 ◽  
Vol 1097 ◽  
pp. 145-150 ◽  
Author(s):  
Yunshen Zhang ◽  
Yichao Huang ◽  
Jiangwei Zhang ◽  
Li Zhu ◽  
Kun Chen ◽  
...  

2019 ◽  
Vol E102.C (11) ◽  
pp. 813-817
Author(s):  
Yosei SHIBATA ◽  
Ryosuke SAITO ◽  
Takahiro ISHINABE ◽  
Hideo FUJIKAKE

2020 ◽  
Author(s):  
Hossein Khalilian ◽  
Gino A. DiLabio

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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