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Article

Role of amino acid hydrophobicity, aromaticity, and molecular volume on IAPP(20-29) amyloid self-assembly.

Proteins - 1 Apr 2012

Doran Todd M, Kamens Alissa J, Byrnes Nadia K, Nilsson Bradley L

Abstract excerpt

Aromatic amino acids strongly promote cross-β amyloid formation; whether the amyloidogenicity of aromatic residues is due to high hydrophobicity and β-sheet propensity or formation of stabilizing π-π interactions has been debated. To clarify the role of aromatic residues on amyloid formation, the islet amyloid polypeptide 20-29 fragment [IAPP(20-29)], which contains a single aromatic residue (Phe 23), was adopted...

Read the complete abstract on PubMed

Topics

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Share to Amino Acids, Aromatic
Share to Amyloid
Share to Hydrophobic and Hydrophilic Interactions

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Islet Amyloid Polypeptide

Share to Leucine

Share to Protein Interaction Mapping

Share to Protein Stability

Share to Spectroscopy, Fourier Transform Infrared

Source

Identifiers

PMID: 22253015
DOI: 10.1002/prot.24007

Genes

IAPP

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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