Evidence map›Paper›PMID 20809197›Full record

ArticleEuropean biophysics journal : EBJ2011

The role of aromatic side-chains in amyloid growth and membrane interaction of the islet amyloid polypeptide fragment LANFLVH.

Danilo Milardi, Michele F M Sciacca, Matteo Pappalardo, Domenico M Grasso, Carmelo La Rosa

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Article in European biophysics journal : EBJ, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

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20citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

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3 · Its place in the literature

Who cites it

20 citing papers in PubMed.

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4 · The record

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5 · Who and what money

Authors and funding

5 authors.

Danilo MilardiIstituto di Biostrutture e Bioimmagini, U.O.S. Catania, Consiglio Nazionale delle Ricerche, Viale Andrea Doria 6, 95125, Catania, Italy.
Michele F M Sciacca
Matteo Pappalardo
Domenico M Grasso
Carmelo La Rosa

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Human islet amyloid polypeptide (hIAPP) is known to misfold and aggregate into amyloid deposits that may be found in pancreatic tissues of patients affected by type 2 diabetes. Recent studies have shown that the highly amyloidogenic peptide LANFLVH, corresponding the N-terminal 12-18 region of IAPP, does not induce membrane damage. Here we assess the role played by the aromatic residue Phe in driving both amyloid formation and membrane interaction of LANFLVH. To this aim, a set of variant heptapeptides in which the aromatic residue Phe has been substituted with a Leu and Ala is studied. Differential scanning calorimetry (DSC) and membrane-leakage experiments demonstrated that Phe substitution noticeably affects the peptide-induced changes in the thermotropic properties of the lipid bilayer but not its membrane damaging potential. Atomic force microscopy (AFM), ThT fluorescence and Congo red birefringence assays evidenced that the Phe residue is not required for fibrillogenesis, but it can influence the self-assembling kinetics. Molecular dynamics simulations have paralleled the outcome of the experimental trials also providing informative details about the structure of the different peptide assemblies. These results support a general theory suggesting that aromatic residues, although capable of affecting the self-assembly kinetics of small peptides and peptide-membrane interactions, are not essential either for amyloid formation or membrane leakage, and indicate that other factors such as β-sheet propensity, size and hydrophobicity of the side chain act synergistically to determine peptide properties.

Indexed as

AlanineAmino Acids, AromaticAmino Acid SequenceCalorimetry, Differential ScanningCell MembraneDiabetes Mellitus, Type 2HumansHydrophobic and Hydrophilic InteractionsIslet Amyloid PolypeptideLeucineLipid BilayersMicroscopy, Atomic ForceMolecular Dynamics SimulationMolecular Sequence DataPeptide FragmentsPhenylalanineAlanineAmino Acids, AromaticIslet Amyloid PolypeptideLeucineLipid BilayersPeptide FragmentsPhenylalanine

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Registered trials

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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.