Recapitulating the α-helix: nonpeptidic, low-molecular-weight ligands for the modulation of helix-mediated protein–protein interactions

2013 ◽  
Vol 5 (18) ◽  
pp. 2157-2174 ◽  
Author(s):  
Maryanna Lanning ◽  
Steven Fletcher
Keyword(s):  
Molecular Weight ◽  
Protein Interactions ◽  
Low Molecular Weight ◽  
Protein Protein Interactions ◽  
Α Helix

Low-molecular-weight spies of protein–protein interactions

2008 ◽  
Vol 11 (4-5) ◽  
pp. 499-505 ◽  
Author(s):  
Jascha Blobel ◽  
Rosa Fayos ◽  
Jesús García ◽  
Oriol Marimon ◽  
Yolanda Pérez ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Protein Interactions ◽  
Low Molecular Weight ◽  
Protein Protein Interactions

scholarly journals Set-up and screening of a fragment library targeting the 14-3-3 protein interface

MedChemComm ◽  
2019 ◽  
Vol 10 (10) ◽  
pp. 1796-1802 ◽  
Author(s):  
Dario Valenti ◽  
João Filipe Neves ◽  
François-Xavier Cantrelle ◽  
Stanimira Hristeva ◽  
Domenico Lentini Santo ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Protein Interactions ◽  
Low Molecular Weight ◽  
Protein Interface ◽  
Protein Protein Interactions ◽  
Fragment Library ◽  
Set Up

Fragment-based driven discovery of 3 new low molecular weight starting points for the modulation of 14-3-3 protein–protein interactions.

Control of Protein−Protein Interactions:  Structure-Based Discovery of Low Molecular Weight Inhibitors of the Interactions between Pin1 WW Domain and Phosphopeptides

2005 ◽  
Vol 48 (15) ◽  
pp. 4815-4823 ◽  
Author(s):  
Caroline Smet ◽  
Jean-Frédéric Duckert ◽  
Jean-Michel Wieruszeski ◽  
Isabelle Landrieu ◽  
Luc Buée ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Protein Interactions ◽  
Low Molecular Weight ◽  
Protein Protein Interactions ◽  
Ww Domain

scholarly journals A Computational Approach to Understand the Interactions Stabilizing the Aβ1-42 Oligomers

2020 ◽  
Vol 11 (2) ◽  
pp. 8804-8817
Keyword(s):  
Structural Dynamics ◽  
Protein Interactions ◽  
Trajectory Analysis ◽  
Low Molecular Weight ◽  
Interaction Study ◽  
Protein Protein Interactions ◽  
Random Coils ◽  
Α Helix ◽  
Dynamics Simulations ◽  
Insight Into

Aβ peptide aggregation is known to be an important factor in the cause of Alzheimer’s disease (AD). Smaller oligomers, the intermediates during the process of aggregation, are known to be more neurotoxic than matured fibrils. To gain the insight into the toxicity of low molecular weight Aβ1-42 oligomers, it is essential to understand the course of its formation and the interactions involved. But the structural dynamics of Aβ1-42 oligomers at the atomistic level and the interactions holding the monomeric units in the oligomeric structures still remain elusive. In this study, using molecular dynamics simulations, we have investigated the structural dynamics of the toxic Aβ1-42 peptide intermediates and the interactions stabilizing the oligomers. From the structural dynamics of Aβ1-42 oligomers, we observed the significant number of secondary structural transitions from α-helix to random coils in some of the monomeric units. From the interaction study, we noticed the involvement of hydrophobic contacts and inter-molecular hydrogen bonds in stabilizing the oligomers. Additionally, we subjected the equilibrated structure of the oligomers in the PDBSum server to examine the protein-protein interactions. The interaction results obtained from the PDBSum server was found to be consistent with the results obtained from the trajectory analysis.

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.

scholarly journals Optimal Anchoring of a Urea-based Foldamer Inhibitor of ASF1 Histone Chaperone Through Backbone Plasticity

2020 ◽  
Author(s):  
Johanne Mbianda ◽  
May Bakail ◽  
Christophe André ◽  
Gwenaëlle Moal ◽  
Marie E. Perrin ◽  
...  
Keyword(s):  
Protein Interactions ◽  
Histone Chaperone ◽  
Protein Protein Interactions ◽  
Protein Surface ◽  
Chromatin Dynamics ◽  
Correct Orientation ◽  
Surface Recognition ◽  
Binding Interface ◽  
Helical Peptide ◽  
Α Helix

<p><b>Sequence-specific oligomers with predictable folding patterns, i.e. foldamers provide new opportunities to mimic α-helical peptides and design inhibitors of protein-protein interactions. One major hurdle of this strategy is to retain the correct orientation of key side chains involved in protein surface recognition. Here, we show that the structural plasticity of a foldamer backbone may significantly contribute to the required spatial adjustment for optimal interaction with the protein surface. By using oligoureas as α-helix mimics, we designed a foldamer/peptide hybrid inhibitor of histone chaperone ASF1, a key regulator of chromatin dynamics. The crystal structure of its complex with ASF1 reveals a striking plasticity of the urea backbone, which adapts to the ASF1 surface to maintain the same binding interface. One additional benefit of generating ASF1 ligands with non-peptide oligourea segments is the resistance to proteolysis in human plasma which was highly improved compared to the cognate α-helical peptide. </b></p>

scholarly journals Correction to α-Helix-Mimicking Sulfono-γ-AApeptide Inhibitors for p53–MDM2/MDMX Protein–Protein Interactions

2020 ◽  
Vol 63 (17) ◽  
pp. 10087-10087
Author(s):  
Peng Sang ◽  
Yan Shi ◽  
Junhao Lu ◽  
Lihong Chen ◽  
Leixiang Yang ◽  
...  
Keyword(s):  
Protein Interactions ◽  
Protein Protein Interactions ◽  
Α Helix
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