Synthesis and pH-responsive properties of pseudo-peptides containing hydrophobic amino acid grafts

2009 ◽  
Vol 19 (24) ◽  
pp. 4217 ◽  
Author(s):  
Rongjun Chen ◽  
Mark E. Eccleston ◽  
Zhilian Yue ◽  
Nigel K. H. Slater
Keyword(s):  
Amino Acid ◽  
Ph Responsive ◽  
Hydrophobic Amino Acid

scholarly journals The role of hydrophobic amino acid grafts in the enhancement of membrane-disruptive activity of pH-responsive pseudo-peptides

Biomaterials ◽  
2009 ◽  
Vol 30 (10) ◽  
pp. 1954-1961 ◽  
Author(s):  
Rongjun Chen ◽  
Sariah Khormaee ◽  
Mark E. Eccleston ◽  
Nigel K.H. Slater
Keyword(s):  
Amino Acid ◽  
Ph Responsive ◽  
Hydrophobic Amino Acid

pH-Responsive self-assembly in an aqueous mixture of surfactant and hydrophobic amino acid mimic

Soft Matter ◽  
2009 ◽  
Vol 5 (15) ◽  
pp. 2919 ◽  
Author(s):  
Gunjan Verma ◽  
Vinod Kumar Aswal ◽  
Puthusserickal Hassan
Keyword(s):  
Amino Acid ◽  
Self Assembly ◽  
Ph Responsive ◽  
Hydrophobic Amino Acid ◽  
Aqueous Mixture

scholarly journals Mitigating the Adverse Effects of Polychlorinated Biphenyl Derivatives on Estrogenic Activity via Molecular Modification Techniques

2021 ◽  
Vol 18 (9) ◽  
pp. 4999
Author(s):  
Wei He ◽  
Wenhui Zhang ◽  
Zhenhua Chu ◽  
Yu Li
Keyword(s):  
Amino Acid ◽  
Binding Site ◽  
Hydrophobic Interaction ◽  
Oestrogen Receptor ◽  
Polychlorinated Biphenyl ◽  
Hydrophobic Interactions ◽  
Estrogenic Activity ◽  
Average Distance ◽  
Amino Acid Residues ◽  
Hydrophobic Amino Acid

The aim of this paper is to explore the mechanism of the change in oestrogenic activity of PCBs molecules before and after modification by designing new PCBs derivatives in combination with molecular docking techniques through the constructed model of oestrogenic activity of PCBs molecules. We found that the weakened hydrophobic interaction between the hydrophobic amino acid residues and hydrophobic substituents at the binding site of PCB derivatives and human oestrogen receptor alpha (hERα) was the main reason for the weakened binding force and reduced anti-oestrogenic activity. It was consistent with the information that the hydrophobic field displayed by the 3D contour maps in the constructed oestrogen activity CoMSIA model was one of the main influencing force fields. The hydrophobic interaction between PCB derivatives and oestrogen-active receptors was negatively correlated with the average distance between hydrophobic substituents and hydrophobic amino acid residues at the hERα-binding site, and positively correlated with the number of hydrophobic amino acid residues. In other words, the smaller the average distance between the hydrophobic amino acid residues at the binding sites between the two and the more the number of them, and the stronger the oestrogen activity expression degree of PCBS derivative molecules. Therefore, hydrophobic interactions between PCB derivatives and the oestrogen receptor can be reduced by altering the microenvironmental conditions in humans. This reduces the ability of PCB derivatives to bind to the oestrogen receptor and can effectively modulate the risk of residual PCB derivatives to produce oestrogenic activity in humans.

Self-Assembly Thermodynamics of pH-Responsive Amino-Acid-Based Polymers with a Nonionic Surfactant

Langmuir ◽  
2014 ◽  
Vol 30 (38) ◽  
pp. 11307-11318 ◽  
Author(s):  
Anna Bogomolova ◽  
Sandro Keller ◽  
Johannes Klingler ◽  
Marian Sedlak ◽  
Dmytro Rak ◽  
...  
Keyword(s):  
Amino Acid ◽  
Nonionic Surfactant ◽  
Self Assembly ◽  
Ph Responsive

Environmentally responsive amino acid-bioconjugated dynamic covalent copolymer as a versatile scaffold for conjugation

RSC Advances ◽  
2015 ◽  
Vol 5 (39) ◽  
pp. 30456-30463 ◽  
Author(s):  
Lin Wang ◽  
Li Liu ◽  
Libin Wu ◽  
Lingzhi Liu ◽  
Xiaobei Wang ◽  
...  
Keyword(s):  
Amino Acid ◽  
Oxidative Coupling ◽  
Click Reaction ◽  
Coupling Reaction ◽  
Ph Responsive ◽  
Oxidative Coupling Reaction ◽  
Environmentally Responsive

A tyrosine-conjugated biodynamer with thermo/pH-responsive and adaptive features is constructed and modified by tyrosine-click reaction and HRP-mediated oxidative coupling reaction.

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