Most proteins fold into their native structure through well defined pathways which involve a limited number of transient intermediates. Intermediates play a relevant role in the folding process; many diseases of genetic nature are in fact coupled with protein misfolding due to formation of stable, inactive intermediate species of the protein. This review deals with a number of diseases associated with protein misfolding and briefly describes the mechanism(s) responsible, at molecular level, for such pathologies. It is also considered the (native ⇆ molten globule) transition, recently observed for some proteins, in which a native protein converts into a stable compact intermediate state able to carry out distinct physiological functions inside the cell. A non-native compact form of cyt c, for example, appears to have a role in the programmed cell death (apoptosis) after that the protein is released from the mitochondrion and non-native forms of the same protein appear involved in some of the disorders attributed to amyloid formation. © 2008 Bentham Science Publishers Ltd.
Santucci, R., Sinibaldi, F., Fiorucci, L. (2008). Protein folding, unfolding and misfolding: Role played by intermediate states. MINI-REVIEWS IN MEDICINAL CHEMISTRY, 8(1), 57-62 [10.2174/138955708783331522].
Protein folding, unfolding and misfolding: Role played by intermediate states
SANTUCCI, ROBERTO;SINIBALDI, FEDERICA;FIORUCCI, LAURA
2008-01-01
Abstract
Most proteins fold into their native structure through well defined pathways which involve a limited number of transient intermediates. Intermediates play a relevant role in the folding process; many diseases of genetic nature are in fact coupled with protein misfolding due to formation of stable, inactive intermediate species of the protein. This review deals with a number of diseases associated with protein misfolding and briefly describes the mechanism(s) responsible, at molecular level, for such pathologies. It is also considered the (native ⇆ molten globule) transition, recently observed for some proteins, in which a native protein converts into a stable compact intermediate state able to carry out distinct physiological functions inside the cell. A non-native compact form of cyt c, for example, appears to have a role in the programmed cell death (apoptosis) after that the protein is released from the mitochondrion and non-native forms of the same protein appear involved in some of the disorders attributed to amyloid formation. © 2008 Bentham Science Publishers Ltd.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.