ArticleThe journal of physical chemistry. B2016
Aggregation of Chameleon Peptides: Implications of α-Helicity in Fibril Formation.
Article in The journal of physical chemistry. B, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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Who cites it
6 citing papers in PubMed, 24 citations in OpenAlex.
- Differential fibril morphologies and thermostability determine functional roles ofFrontiers in molecular biosciences · 2023Article
- The amphibian antimicrobial peptide uperin 3.5 is a cross-α/cross-β chameleon functional amyloid.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Structure of the Hydrophobic Core Determines the 3D Protein Structure-Verification by Single Mutation Proteins.Biomolecules · 2020Article
- Kinetic and thermodynamic study of beta-Boswellic acid interaction with Tau protein investigated by surface plasmon resonance and molecular modeling methods.BioImpacts : BI · 2020Article
- The Role of Buffers in Wild-Type HEWL Amyloid Fibril Formation Mechanism.Biomolecules · 2019Article
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Authors and funding
6 authors.
Funding
Abstract
We investigate the relationship between the inherent secondary structure and aggregation propensity of peptides containing chameleon sequences (i.e., sequences that can adopt either α or β structure depending on context) using a combination of replica exchange molecular dynamics simulations, ion-mobility mass spectrometry, circular dichroism, and transmission electron microscopy. We focus on an eight-residue long chameleon sequence that can adopt an α-helical structure in the context of the iron-binding protein from Bacillus anthracis (PDB id 1JIG ) and a β-strand in the context of the baculovirus P35 protein (PDB id 1P35 ). We show that the isolated chameleon sequence is intrinsically disordered, interconverting between α-helical and β-rich conformations. The inherent conformational plasticity of the sequence can be constrained by addition of flanking residues with a given secondary structure propensity. Intriguingly, we show that the chameleon sequence with helical flanking residues aggregates rapidly into fibrils, whereas the chameleon sequence with flanking residues that favor β-conformations has weak aggregation propensity. This work sheds new insights into the possible role of α-helical intermediates in fibril formation.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.