ChemInform Abstract: The Development of a Modular Synthesis of Teraryl-Based α-Helix Mimetics as Potential Inhibitors of Protein-Protein Interactions

ChemInform ◽  
2014 ◽  
Vol 45 (36) ◽  
pp. no-no ◽  
Author(s):  
Melanie Trobe ◽  
Martin Peters ◽  
Sebastian H. Grimm ◽  
Rolf Breinbauer
Keyword(s):  
Protein Interactions ◽  
Protein Protein Interactions ◽  
Modular Synthesis ◽  
Helix Mimetics ◽  
Α Helix ◽  
Potential Inhibitors

α-Helix mimetics as inhibitors of protein–protein interactions

2008 ◽  
Vol 36 (6) ◽  
pp. 1414-1417 ◽  
Author(s):  
Ishu Saraogi ◽  
Andrew D. Hamilton
Keyword(s):  
Protein Interactions ◽  
First Generation ◽  
Side Chain ◽  
Protein Protein Interactions ◽  
Substitution Pattern ◽  
Pathological Conditions ◽  
Synthetic Accessibility ◽  
Helix Mimetics ◽  
Viable Approach ◽  
Α Helix

The inhibition of protein–protein interactions using small molecules is a viable approach for the treatment of a range of pathological conditions that result from a malfunctioning of these interactions. Our strategy for the design of such agents involves the mimicry of side-chain residues on one face of the α-helix; these residues frequently play a key role in mediating protein–protein interactions. The first-generation terphenyl scaffold, with a 3,2′,2″-substitution pattern, is able to successfully mimic key helix residues and disrupt therapeutically relevant interactions, including the Bcl-XL–Bak and the p53–hDM2 (human double minute 2) interactions that are implicated in cancer. The second- and third-generation scaffolds have resulted in greater synthetic accessibility and more drug-like character in these molecules.

scholarly journals Heterocyclic α-helix mimetics for targeting protein–protein interactions

2007 ◽  
Vol 17 (16) ◽  
pp. 4641-4645 ◽  
Author(s):  
Shannon M. Biros ◽  
Lionel Moisan ◽  
Enrique Mann ◽  
Alexandre Carella ◽  
Dayong Zhai ◽  
...  
Keyword(s):  
Protein Interactions ◽  
Protein Protein Interactions ◽  
Helix Mimetics ◽  
Α Helix

Converting One-Face α-Helix Mimetics into Amphiphilic α-Helix Mimetics as Potent Inhibitors of Protein–Protein Interactions

2015 ◽  
Vol 18 (1) ◽  
pp. 36-42 ◽  
Author(s):  
Ji Hoon Lee ◽  
Misook Oh ◽  
Hyun Soo Kim ◽  
Huisun Lee ◽  
Wonpil Im ◽  
...  
Keyword(s):  
Protein Interactions ◽  
Protein Protein Interactions ◽  
Helix Mimetics ◽  
Α Helix

scholarly journals Novel Pyrrolopyrimidine-Based α-Helix Mimetics: Cell-Permeable Inhibitors of Protein−Protein Interactions

2011 ◽  
Vol 133 (4) ◽  
pp. 676-679 ◽  
Author(s):  
Ji Hoon Lee ◽  
Qi Zhang ◽  
Sunhwan Jo ◽  
Sergio C. Chai ◽  
Misook Oh ◽  
...  
Keyword(s):  
Protein Interactions ◽  
Protein Protein Interactions ◽  
Helix Mimetics ◽  
Α Helix

scholarly journals Peptide-based inhibitors of protein–protein interactions: biophysical, structural and cellular consequences of introducing a constraint

2021 ◽  
Author(s):  
Hongshuang Wang ◽  
Robert S. Dawber ◽  
Peiyu Zhang ◽  
Martin Walko ◽  
Andrew J. Wilson ◽  
...  
Keyword(s):  
Protein Interactions ◽  
Protein Protein Interactions ◽  
Α Helix ◽  
Cellular Behaviour

This review summarizes the influence of inserting constraints on biophysical, conformational, structural and cellular behaviour for peptides targeting α-helix mediated protein–protein interactions.

scholarly journals Interactions between Integrase and Excisionase in the Phage Lambda Excisive Nucleoprotein Complex

2002 ◽  
Vol 184 (18) ◽  
pp. 5200-5203 ◽  
Author(s):  
Eun Hee Cho ◽  
Richard I. Gumport ◽  
Jeffrey F. Gardner
Keyword(s):  
Protein Interactions ◽  
Protein Protein Interactions ◽  
Mobility Shift ◽  
Host Chromosome ◽  
Amino Terminal ◽  
Nucleoprotein Complex ◽  
Carboxyl Terminal ◽  
Α Helix ◽  
Gel Mobility Shift ◽  
Amino Terminal Domain

ABSTRACT Bacteriophage lambda site-specific recombination comprises two overall reactions, integration into and excision from the host chromosome. Lambda integrase (Int) carries out both reactions. During excision, excisionase (Xis) helps Int to bind DNA and introduces a bend in the DNA that facilitates formation of the proper excisive nucleoprotein complex. The carboxyl-terminal α-helix of Xis is thought to interact with Int through direct protein-protein interactions. In this study, we used gel mobility shift assays to show that the amino-terminal domain of Int maintained cooperative interactions with Xis. This finding indicates that the amino-terminal arm-type DNA binding domain of Int interacts with Xis.

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