Role of Urea–Aromatic Stacking Interactions in Stabilizing the Aromatic Residues of the Protein in Urea-Induced Denatured State

2017 ◽  
Vol 139 (42) ◽  
pp. 14931-14946 ◽  
Author(s):  
Siddharth Goyal ◽  
Aditya Chattopadhyay ◽  
Koushik Kasavajhala ◽  
U. Deva Priyakumar
Keyword(s):  
Stacking Interactions ◽  
Denatured State ◽  
Aromatic Residues ◽  
Aromatic Stacking

scholarly journals Structure of Musashi1 in a complex with target RNA: the role of aromatic stacking interactions

2011 ◽  
Vol 40 (7) ◽  
pp. 3218-3231 ◽  
Author(s):  
Takako Ohyama ◽  
Takashi Nagata ◽  
Kengo Tsuda ◽  
Naohiro Kobayashi ◽  
Takao Imai ◽  
...  
Keyword(s):  
Stacking Interactions ◽  
Aromatic Stacking ◽  
Target Rna

A Chemical Perspective to the Anti-Amyloid Action of Compounds and a Nanoparticle Based Assay for Screening Amyloid Inhibitors

2020 ◽  
Author(s):  
Nidhi Gour ◽  
Bharti Koshti
Keyword(s):  
Memory Loss ◽  
Cost Effective ◽  
Structural Motif ◽  
Rapid Screening ◽  
Stacking Interactions ◽  
Aromatic Rings ◽  
Amyloid Fibers ◽  
Aromatic Stacking ◽  
Cost Effective Technique ◽  
The Brain

Aggregation of amyloid beeta 1-42 (Aβ<sub>42</sub>) peptide causes the formation of clustered deposits knows as amyloid plaques in the brain which leads to neuronal dysfunction and memory loss and associated with many neurological disorders including Alzheimer’s and Parkinson’s. Aβ<sub>42</sub> has core structural motif with phenylalanine at the 19 and 20 positions. The diphenylalanine (FF) residue plays a crucial role in the formation of amyloid fibers and serves as model peptide for studying Aβ<sub>42 </sub>aggregation. FF self-assembles to well-ordered tubular morphology via aromatic pi-pi stackings. Our studies, suggest that the aromatic rings present in the anti-amyloidogenic compounds may interact with the pi-pi stacking interactions present in the FF. Even the compounds which do not have aromatic rings, like cyclodextrin and cucurbituril show anti-amyloid property due to the binding of aromatic ring inside the guest cavity. Hence, our studies also suggest that compounds which may have a functional moiety capable of interacting with the aromatic stacking interactions might be tested for their anti-amyloidogenic properties. Further, in this manuscript, we have proposed two novel nanoparticle based assays for the rapid screening of amyloid inhibitors. In the first assay, interaction between biotin-tagged FF peptide and the streptavidin labelled gold nanoparticles (s-AuNPs) were used. In another assay, thiol-Au interactions were used to develop an assay for detection of amyloid inhibitors. It is envisaged that the proposed analytical method will provide a simple, facile and cost effective technique for the screening of amyloid inhibitors and may be of immense practical implications to find the therapeutic remedies for the diseases associated with the protein aggregation.

scholarly journals The role of aromatic residues in the hydrophobic core of the villin headpiece subdomain

2009 ◽  
Vol 11 (3) ◽  
pp. 680-687 ◽  
Author(s):  
Benjamin S. Frank ◽  
Didem Vardar ◽  
Deirdre A. Buckley ◽  
C. James McKnight
Keyword(s):  
Hydrophobic Core ◽  
Villin Headpiece ◽  
Aromatic Residues

Role of aromatic residues in the structure-function relationship of .alpha.-bungarotoxin

Biochemistry ◽  
1982 ◽  
Vol 21 (11) ◽  
pp. 2592-2600 ◽  
Author(s):  
Yee Hsiung Chen ◽  
Jang Chyi Tai ◽  
Wan Jen Huang ◽  
Ming Zong Lai ◽  
Mien Chie Hung ◽  
...  
Keyword(s):  
Structure Function ◽  
Aromatic Residues ◽  
Structure Function Relationship ◽  
Function Relationship ◽  
Alpha Bungarotoxin ◽  
Relationship Of
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