Next Article in Journal
Species-specific Fungal DNA in Airborne Dust as Surrogate for Occupational Mycotoxin Exposure?
Next Article in Special Issue
Folding, Stability and Shape of Proteins in Crowded Environments: Experimental and Computational Approaches
Previous Article in Journal
A Nutritional Approach for the Management of Deoxynivalenol (DON) Toxicity in the Gastrointestinal Tract of Growing Chickens
Previous Article in Special Issue
Discovery of Proteomic Code with mRNA Assisted Protein Folding
Article Menu

Export Article

Open AccessReview
Int. J. Mol. Sci. 2008, 9(12), 2515-2542;

Protein Folding and Misfolding on Surfaces

Department of Biochemical Sciences and Research Centre on the Molecular Basis of Neurodegeneration (CIMN), University of Florence, Florence, Italy
Received: 6 November 2008 / Revised: 3 December 2008 / Accepted: 8 December 2008 / Published: 10 December 2008
(This article belongs to the Special Issue Protein Folding 2009)
Full-Text   |   PDF [1053 KB, uploaded 19 June 2014]


Protein folding, misfolding and aggregation, as well as the way misfolded and aggregated proteins affects cell viability are emerging as key themes in molecular and structural biology and in molecular medicine. Recent advances in the knowledge of the biophysical basis of protein folding have led to propose the energy landscape theory which provides a consistent framework to better understand how a protein folds rapidly and efficiently to the compact, biologically active structure. The increased knowledge on protein folding has highlighted its strict relation to protein misfolding and aggregation, either process being in close competition with the other, both relying on the same physicochemical basis. The theory has also provided information to better understand the structural and environmental factors affecting protein folding resulting in protein misfolding and aggregation into ordered or disordered polymeric assemblies. Among these, particular importance is given to the effects of surfaces. The latter, in some cases make possible rapid and efficient protein folding but most often recruit proteins/peptides increasing their local concentration thus favouring misfolding and accelerating the rate of nucleation. It is also emerging that surfaces can modify the path of protein misfolding and aggregation generating oligomers and polymers structurally different from those arising in the bulk solution and endowed with different physical properties and cytotoxicities. View Full-Text
Keywords: Protein folding; protein misfolding; protein aggregation; amyloid; amyloid fibrils; amyloid cytotoxicity Protein folding; protein misfolding; protein aggregation; amyloid; amyloid fibrils; amyloid cytotoxicity
This is an open access article distributed under the Creative Commons Attribution License (CC BY 3.0).

Share & Cite This Article

MDPI and ACS Style

Stefani, M. Protein Folding and Misfolding on Surfaces. Int. J. Mol. Sci. 2008, 9, 2515-2542.

Show more citation formats Show less citations formats

Related Articles

Article Metrics

Article Access Statistics



[Return to top]
Int. J. Mol. Sci. EISSN 1422-0067 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
Back to Top