Utilize este identificador para referenciar este registo: http://hdl.handle.net/10451/21548
Título: Protein misfolding in conformational disorders
Rescue of folding defects and chemical chaperoning
Autor: Leandro, Paula
Gomes, Claudio M.
Palavras-chave: Chemistry, Medicinal
Data: 2008
Citação: MINI-REVIEWS IN MEDICINAL CHEMISTRY. - Vol. 8, n. 9 (AUG 2008), p. 901-911
Resumo: Protein folding in the cell is a tightly regulated process, involving a series of proteins, from molecular chaperones to proteases that assist the folding process and monitor the quality of the final product. Despite this control, genetic or sporadic factors may compromise protein folding and the folded state resulting in the formation of non-native misfolded, destabilised, aggregated or fibrillar species. These are hallmarks of the so-called protein conformational disorders, in which the altered protein conformations result in cell toxicity, functional deficiency or lead to dominant negative effects. Examples of such pathologies include neurodegenerative and metabolic disorders. In recent years, it has become clear that several different small chemical compounds such as osmolytes, protein inhibitors, ligands and cofactors exert a chemical chaperoning effect and are able to rescue folding and trafficking defects, minimising or partly overcoming the pathological consequences of protein misfolding. Here we review the different types of chemical chaperones and provide a structural and energetic rationale for their action. Examples of chemical chaperoning are overviewed and discussed on the basis of the reported effects exerted by chemical compounds at different stages of the protein folding process and protein conformational states.. - Fundacao para a Ciencia e Tecnologia (FCT/MCTES). - C. Rodrigues-Pousada and T. Bandeiras (ITQB) are gratefully acknowledged for critically reading of the manuscript and for insightful comments. H. Botelho is gratefully acknowledged for data and assistance on (Fig. 5). Funding from the Fundacao para a Ciencia e Tecnologia (FCT/MCTES) is gratefully acknowledged.
URI: http://hdl.handle.net/10451/21548
ISSN: 1389-5575
Aparece nas colecções:FF - Produção Científica 2000-2009

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