Self-assembly and aggregation of proteins

https://doi.org/10.1016/j.cocis.2007.07.010Get rights and content

Abstract

Recent work on the assembly of small peptides and of proteins into linear and non-linear aggregates is addressed and discussed in view of the challenges in describing food protein assembly.

Section snippets

Major recent advances

On the level of single peptides the influence of chemical groups on fibrillisation is being studied, elaborating on recent advances in X-ray microcrystallography. On the level of proteins the various pathways towards fibrillisation are being unraveled including the influence of protein hydrolysis.

Linear structures: amyloids and amyloid-like assemblies

Amyloid fibrils (related to disease) and amyloid-like fibrils share some structural properties, such as the presence of β-sheets orthogonal to the fibril axis. Knowledge of the mechanisms of amyloid(-like) formation leading to predictive models is desirable, in particular on a structural molecular level. This is necessary in order to prevent amyloidosis, as nicely reviewed by Sciaretta et al. [1], as well as in order to utilize amyloid-like fibrils. Fibrils can be utilized as gelling materials,

Spherulites

A spherulite is a spherical ordered structure that results in a Maltese extinction pattern when observed between crossed polarisers through a light microscope. Spherulite formation also is observed during polymer crystallisation and during crystallisation of metals. Several proteins which are reported to exhibit such structures, which range up to millimetres in size. They include bovine insulin [62] and β-lactoglobulin [63], [64]. Interestingly, two peptides, one being cyclic and one being

Conclusions

Since the assembly of proteins is ubiquitous, the subject receives a considerable attention from various disciplines. Many different structures, varying in size as well as in shape, can be formed depending on the exact conditions when they are formed. This leads to the opportunity to engineer structures with certain desirable properties. Linear structures like amyloids and amyloid-like fibrils form an interesting class for studying for their importance in the medical field, but also have

Acknowledgement

We gratefully acknowledge the assistance of Mrs. E. Jansen in the preparation of the manuscript.

References (80)

  • J.M. Smeenk et al.

    Fibril formation by triblock copolymers of silklike β-sheet polypeptides and poly(ethylene glycol)

    Macromolecules

    (2006)
  • S.G. Bolder et al.

    Heat-induced whey protein isolate fibrils: conversion, hydrolysis, and disulphide bond formation

    Int Dairy J

    (2007)
  • M. Fändrich et al.

    Apomyoglobin reveals a random-nucleation mechanism in amyloid protofibril formation

    Acta Histochem

    (2006)
  • S. Kumar et al.

    Mechanism of formation of amyloid protofibrils of barstar from soluble oligomers: evidence for multiple steps and lateral association coupled to conformational conversion

    J Mol Biol

    (2007)
  • K. Broersen et al.

    Effect of protein charge on the generation of aggregation-prone conformers

    BioMacromolecules

    (2007)
  • T.R. Jahn et al.

    Amyloid formation under physiological conditions proceeds via a native-like folding intermediate

    Nat Struct Mol Biol

    (2006)
  • T. Koga et al.

    Controlled self-assembly of amphiphilic oligopeptides into shape-specific nanoarchitectures

    Chem — Eur J

    (2006)
  • X. Zhao et al.

    Designer self-assembling peptide materials

    Macromol Biosci

    (2007)
  • I.C. Reynhout et al.

    Self-assembled architectures from biohybrid triblock copolymers

    J Am Chem Soc

    (2007)
  • N. Sanchez de Groot et al.

    Ile–Phe dipeptide self-assembly: clues to amyloid formation

    Biophys J

    (2007)
  • K. Huang et al.

    Structure-specific effects of protein topology on cross-β assembly: studies of insulin fibrillation

    Biochemistry

    (2006)
  • Y. Porat et al.

    Inhibition of amyloid fibril formation by polyphenols: structural similarity and aromatic interactions as a common inhibition mechanism

    Chem Biol Drug Des

    (2006)
  • E.H.C. Bromley et al.

    Aggregation across the lengthscales in b-lactoglobulin

    Faraday Discuss

    (2005)
  • M. Pouzot et al.

    Influence of the ionic strength on the structure of heat-set globular protein gels at pH 7. β-lactoglobulin

    Macromolecules

    (2004)
  • L. Donato et al.

    Influence of the NaCl or CaCl2 concentration on the structure of heat-set bovine serum albumin gels at pH 7

    BioMacromolecules

    (2005)
  • T. Nicolai et al.

    Iso-scattering points during heat-induced aggregation and gelation of globular proteins indicating micro-phase separation

    Europhys Lett

    (2006)
  • E. Gazit

    Use of biomolecular templates for the fabrication of metal nanowires

    FEBS J

    (2007)
  • S.S. Rogers et al.

    Measuring the length distribution of a fibril system: a flow birefringence technique applied to amyloid fibrils

    Macromolecules

    (2005)
  • S.S. Rogers et al.

    Electric birefringence study of an amyloid fibril system: the short end of the length distribution

    Eur Phys J, E Soft Matter

    (2005)
  • A. Lomakin et al.

    Quasielastic light scattering for protein assembly studies

  • A. Lomakin et al.

    Quasielastic light scattering study of amyloid β-protein fibril formation

    Protein Pept Lett

    (2006)
  • C. Avidan-Shpalter et al.

    The early stages of amyloid formation: biophysical and structural characterization of human calcitonin pre-fibrillar assemblies

    Amyloid

    (2006)
  • F. Meersman et al.

    Probing the pressure–temperature stability of amyloid fibrils provides new insights into their molecular properties

    Biochim Biophys Acta (BBA) — Proteins & Proteomics

    (2006)
  • M.R.H. Krebs et al.

    The mechanism of amyloid spherulite formation by bovine insulin

    Biophys J

    (2005)
  • V. Berthelier et al.

    Screening for modulators of aggregation with a microplate elongation assay

  • M.R.H. Krebs et al.

    Formation and seeding of amyloid fibrils from wild-type hen lysozyme and a peptide fragment from the a-domain

    J Mol Biol

    (2000)
  • R. Wetzel

    Kinetics and thermodynamics of amyloid fibril assembly

    Acc Chem Res

    (2006)
  • L.N. Arnaudov et al.

    Theoretical modeling of the kinetics of fibrilar aggregation of bovine-lactoglobulin at pH 2

    J Chem Phys

    (2007)
  • G. Zandomeneghi et al.

    FTIR reveals structural differences between native b-sheet proteins and amyloid fibrils

    Protein Sci

    (2004)
  • E. Laurine et al.

    Lithostathine quadruple-helical filaments form proteinase k-resistant deposits in Creutzfeldt–Jakob disease

    J Biol Chem

    (2003)
  • Cited by (157)

    View all citing articles on Scopus
    View full text