Biochemical and functional characterization of intrinsically disordered proteins (IDPs) in human diseases
Contact person: Simona Maria Monti, marmonti
unina.it
Actors: Giuseppina De Simone, giuseppina.desimonecnr.it, Vincenzo Alterio, vincenzo.alterio@ibb.cnr.it, Katia D'Ambrosio, katia.dambrosiocnr.it, Anna Di Fiore, anna.difiorecnr.it, Martina Buonanno, martina.buonannocnr.it, Emma Langella, emma.langellacnr.it, Simona Maria Monti, marmontiunina.it,
Research areas: Macromolecules for biomedical and biotechnological applications, Structure and function of proteins involved in physio-pathologic processes,
Contact person: Simona Maria Monti, marmonti
unina.itActors: Giuseppina De Simone, giuseppina.desimone
cnr.it, Vincenzo Alterio, vincenzo.alterio@ibb.cnr.it, Katia D'Ambrosio, katia.dambrosiocnr.it, Anna Di Fiore, anna.difiorecnr.it, Martina Buonanno, martina.buonannocnr.it, Emma Langella, emma.langellacnr.it, Simona Maria Monti, marmontiunina.it, Description:
It is now clearly established that some proteins orprotein regions are devoid of any stable secondary and/or tertiary structureunder physiological conditions, but still possess fundamental biologicalfunctions. These intrinsically disordered proteins (IDPs) or regions (IDRs)have peculiar features due to their plasticity as the capacity of binding theirbiological targets with high specificity and low affinity, and the possibilityof interaction with numerous partners. IDPs and IDRs are especially prevalentin eukaryotes suggesting the necessity of disorder, associated to signallingand regulation processes in nucleated cells where they are involved in many keyfunctions. However, also a correlation between intrinsic disorder and varioushuman diseases such as cancer, diabetes, amyloidosis and neurodegenerativediseases is now evident, highlighting the great importance of this issue which necessitatesto be further investigated by means of biochemical, biophysical and computationaltools. Starting from the study of an IDR of a tumour associated protein, namelythe human Carbonic Anhydrase IX, we have extended the investigation on othernatively unfolded proteins or region involved into human diseases.
It is now clearly established that some proteins orprotein regions are devoid of any stable secondary and/or tertiary structureunder physiological conditions, but still possess fundamental biologicalfunctions. These intrinsically disordered proteins (IDPs) or regions (IDRs)have peculiar features due to their plasticity as the capacity of binding theirbiological targets with high specificity and low affinity, and the possibilityof interaction with numerous partners. IDPs and IDRs are especially prevalentin eukaryotes suggesting the necessity of disorder, associated to signallingand regulation processes in nucleated cells where they are involved in many keyfunctions. However, also a correlation between intrinsic disorder and varioushuman diseases such as cancer, diabetes, amyloidosis and neurodegenerativediseases is now evident, highlighting the great importance of this issue which necessitatesto be further investigated by means of biochemical, biophysical and computationaltools. Starting from the study of an IDR of a tumour associated protein, namelythe human Carbonic Anhydrase IX, we have extended the investigation on othernatively unfolded proteins or region involved into human diseases.
Selected papers:
1.
Langella E, Buonanno M et al.,Biochemical, biophysical and molecular dynamics studies on theproteoglycan-like domain of carbonic anhydrase IX . Cell Mol Life Sci. 2018,75, 3283-3296. doi: 10.1007/s00018-018-2798-8
2.
Langella E, Buonanno M et al.,Intrinsically Disordered Features of Carbonic Anhydrase IX Proteoglycan-LikeDomain, Cell Mol Life Sci. 2020 Accepted for publication
Biochemical and functional characterization of intrinsically disordered proteins (IDPs) in human diseases
Biochemical and functional characterization of intrinsically disordered proteins (IDPs) in human diseases
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