Folding mechanisms steer the amyloid fibril formation propensity of highly homologous proteins (466 views) (PDF public 109 views)
Chem Sci (ISSN: 2041-6520linking, 2041-6520print, 2041-6539), 2018 Apr 7; 9(13): 3290-3298.
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Impact factor: 9.063, 5-year impact factor: 8.733
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Affiliations:
*** IBB - CNR ***
Department of Environmental, Biological and Pharmaceutical Sciences and Technologies , University of Campania "Luigi Vanvitelli" , Via Vivaldi 43 , 81100 Caserta , Italy . Email: roberto.fattorusso@unicampania.it.
Institute of Biostructures and Bioimaging , CNR , Via Mezzocannone 16 , 80134 Naples , Italy.
Department of Biochemical Sciences "Alessandro Rossi Fanelli" , University of Rome "La Sapienza" , Piazzale Aldo Moro 5 , 00185 , Roma , Italy.
Institute of Genetics and Biophysics "Adriano Buzzati-Traverso" , CNR , Via P. Castellino 111 , 80131 Napoli , Italy.
Department of Clinical Sciences and Translational Medicine , University of Rome "Tor Vergata" , Via Montpellier 1 , 00133 , Roma , Italy.
References:
Not available.
Chem Sci (ISSN: 2041-6520linking, 2041-6520print, 2041-6539), 2018 Apr 7; 9(13): 3290-3298.
Export to BibTeX Export to EndNote
Paper type: Journal Article,
Impact factor: 9.063, 5-year impact factor: 8.733
Url: Not available.
Keywords: Not available.
Affiliations:
*** IBB - CNR ***
Department of Environmental, Biological and Pharmaceutical Sciences and Technologies , University of Campania "Luigi Vanvitelli" , Via Vivaldi 43 , 81100 Caserta , Italy . Email: roberto.fattorusso@unicampania.it.
Institute of Biostructures and Bioimaging , CNR , Via Mezzocannone 16 , 80134 Naples , Italy.
Department of Biochemical Sciences "Alessandro Rossi Fanelli" , University of Rome "La Sapienza" , Piazzale Aldo Moro 5 , 00185 , Roma , Italy.
Institute of Genetics and Biophysics "Adriano Buzzati-Traverso" , CNR , Via P. Castellino 111 , 80131 Napoli , Italy.
Department of Clinical Sciences and Translational Medicine , University of Rome "Tor Vergata" , Via Montpellier 1 , 00133 , Roma , Italy.
References:
Not available.
Folding mechanisms steer the amyloid fibril formation propensity of highly homologous proteins
Significant advances in the understanding of the molecular determinants of fibrillogenesis can be expected from comparative studies of the aggregation propensities of proteins with highly homologous structures but different folding pathways. Here, we fully characterize, by means of stopped-flow, T-jump, CD and DSC experiments, the unfolding mechanisms of three highly homologous proteins, zinc binding Ros87 and Ml1(53-149) and zinc-lacking Ml4(52-151). The results indicate that the three proteins significantly differ in terms of stability and (un)folding mechanisms. Particularly, Ros87 and Ml1(53-149) appear to be much more stable to guanidine denaturation and are characterized by folding mechanisms including the presence of an intermediate. On the other hand, metal lacking Ml4(52-151) folds according to a classic two-state model. Successively, we have monitored the capabilities of Ros87, Ml4(52-151) and Ml1(53-149) to form amyloid fibrils under native conditions. Particularly, we show, by CD, fluorescence, DLS, TEM and SEM experiments, that after 168 hours, amyloid formation of Ros87 has started, while Ml1(53-149) has formed only amorphous aggregates and Ml4(52-151) is still monomeric in solution. This study shows how metal binding can influence protein folding pathways and thereby control conformational accessibility to aggregation-prone states, which in turn changes aggregation kinetics, shedding light on the role of metal ions in the development of protein deposition diseases.
Significant advances in the understanding of the molecular determinants of fibrillogenesis can be expected from comparative studies of the aggregation propensities of proteins with highly homologous structures but different folding pathways. Here, we fully characterize, by means of stopped-flow, T-jump, CD and DSC experiments, the unfolding mechanisms of three highly homologous proteins, zinc binding Ros87 and Ml1(53-149) and zinc-lacking Ml4(52-151). The results indicate that the three proteins significantly differ in terms of stability and (un)folding mechanisms. Particularly, Ros87 and Ml1(53-149) appear to be much more stable to guanidine denaturation and are characterized by folding mechanisms including the presence of an intermediate. On the other hand, metal lacking Ml4(52-151) folds according to a classic two-state model. Successively, we have monitored the capabilities of Ros87, Ml4(52-151) and Ml1(53-149) to form amyloid fibrils under native conditions. Particularly, we show, by CD, fluorescence, DLS, TEM and SEM experiments, that after 168 hours, amyloid formation of Ros87 has started, while Ml1(53-149) has formed only amorphous aggregates and Ml4(52-151) is still monomeric in solution. This study shows how metal binding can influence protein folding pathways and thereby control conformational accessibility to aggregation-prone states, which in turn changes aggregation kinetics, shedding light on the role of metal ions in the development of protein deposition diseases.
Folding mechanisms steer the amyloid fibril formation propensity of highly homologous proteins
Folding mechanisms steer the amyloid fibril formation propensity of highly homologous proteins
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View Export to BibTeX Export to EndNote
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View Export to BibTeX Export to EndNote
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Iommelli F, De Rosa V, Gargiulo S, Panico M, Monti M, Gramanzini M, Fonti R, Del Vecchio S
* Monitoring Reversal of Concurrent Mechanisms of Resistance to EGFR TKIs in Non-Small Cell Lung Cancer by 18F-FLT PET/CT (333 views)
Eur J Nucl Med (ISSN: 1619-7070, 1619-7089, 1619-7070print), 2014 Oct; 41: N/D-N/D.
Impact Factor: 5.383
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Acampa W, Petretta M, Cuocolo R, Daniele S, Cantoni V, Cuocolo A
* Warranty period of normal stress myocardial perfusion imaging in diabetic patients: A propensity score analysis (575 views)
J Nucl Cardiol (ISSN: 1071-3581, 1532-6551, 1532-6551electronic), 2014 Feb; 21(1): 50-56.
Impact Factor: 2.942
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Bergamo P, Cocca E, Palumbo R, Gogliettino M, Rossi M, Palmieri G
* RedOx status, proteasome and APEH: Insights into anticancer mechanisms of t10, c12-conjugated linoleic acid isomer on A375 melanoma cells (877 views)
Plosone (ISSN: 1932-6203, 1932-6203electronic, 1932-6203linking), 2013 Nov 19; 8(11): N/D-N/D.
Impact Factor: 3.534
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Zampella E, Acampa W, Petretta M, Daniele S, Assante R, Plaitano M, Cantoni V, Cuocolo A
* Warranty Period of Normal Stress Myocardial Perfusion Imaging in Diabetic and Non-diabetic Patients: a Propensity Score Analysis (358 views)
Eur J Nucl Med (ISSN: 1619-7070, 1619-7089, 0340-6997), 2013 Oct; 40: N/D-N/D.
Impact Factor: 5.217
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Palmieri M, Malgieri G, Russo L, Baglivo I, Esposito S, Netti F, Del Gatto A, De Paola I, Zaccaro L, Pedone PV, Isernia C, Milardi D, Fattorusso R
* Structural Zn(II) Implies a Switch from Fully Cooperative to Partly Downhill Folding in Highly Homologous Proteins (464 views)
J Am Chem Soc (ISSN: 0002-7863, 0002-2786, 1520-5126), 2013 Apr 2; 135(13): 5220-5228.
Impact Factor: 11.444
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Sciacca MFM, Milardi D, Messina GML, Marletta G, Brender JR, Ramamoorthy A, La Rosa C
* Cations as switches of amyloid-mediated membrane disruption mechanisms: Calcium and IAPP (678 views)
Biophysical Journal (ISSN: 0006-3495, 1542-0086), 2013 Jan 8; 104(1): 173-184.
Impact Factor: 3.832
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Pirone L, Esposito C, Correale S, Graziano G, Di Gaetano S, Vitagliano L, Pedone E
* Thermal and chemical stability of two homologous POZ/BTB domains of KCTD proteins characterized by a different oligomeric organization (600 views)
Biomed Res Int (ISSN: 2314-6133, 2314-6141, 2314-6141electronic), 2013; 2013: 162674-162674.
Impact Factor: 1.579
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Galdiero S, Russo L, Falanga A, Cantisani M, Vitiello M, Fattorusso R, Malgieri G, Galdiero M, Isernia C
* Structure and Orientation of the gH625-644 Membrane Interacting Region of Herpes Simplex Virus Type 1 in a Membrane Mimetic System (554 views)
Biochemistry (ISSN: 0006-2960, 1520-4995, 1520-4995electronic), 2012 Apr 10; 51(14): 3121-3128.
Impact Factor: 3.377
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D'Auria G, Vacatello M, Falcigno L, Paduano L, Mangiapia G, Calvanese L, Gambaretto R, Dettin M, Paolillo L
* Self-assembling properties of ionic-complementary peptides (729 views)
J Pept Sci (ISSN: 1075-2617, 1099-1387, 1075-2617print), 2009 Mar; 15(3): 210-219.
Impact Factor: 1.807
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Galdiero S, Falanga A, Vitiello M, Raiola L, Fattorusso R, Browne H, Pedone C, Isernia C, Galdiero M
* Analysis of a membrane interacting region of herpes simplex virus type 1 glycoprotein (1157 views)
Jbc Papers (ISSN: 0021-9258, 1083-351x, 0021-9258linking), 2008 Oct 31; 283(44): 29993-30009.
Impact Factor: 5.52
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Mercier Y, Santoro F, Reguero M, Improta R
* The decay from the dark nπ* excited state in uracil: An integrated CASPT2/CASSCF and PCM/TD-DFT study in the gas phase and in water (446 views)
J Phys Chem B (ISSN: 1520-6106, 1520-5207, 1520-5207electronic), 2008 Sep 4; 112(35): 10769-10772.
Impact Factor: 4.189
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Cucinotta V, Giuffrida A, Maccarrone G, Messina M, Puglisi A, Rizzarelli E, Vecchio G
* Coordination properties of 3-functionalized β-cyclodextrins. Thermodynamic stereoselectivity of copper(II) complexes of the A, B-diamino derivative and its exploitation in LECE (418 views)
Dalton T (ISSN: 1477-9226, 1477-9234, 1477-9234electronic), 2005 Sep 21; (16): 2731-2736.
Impact Factor: 3.003
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Di Natale G, Impellizzeri G, Pappalardo G
* Conformational properties of peptide fragments homologous to the 106-114 and 106-126 residues of the human prion protein: a CD and NMR spectroscopic study (504 views)
Org Biomol Chem (ISSN: 1477-0520, 1477-0539, 1477-0539electronic), 2005 Feb 7; 3(3): 490-497.
Impact Factor: 2.547
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Petretta M, Vicario ML, Spinelli L, Ferro A, Cuocolo A, Condorelli M, Bonaduce D
* Combined effect of the force-frequency and length-tension mechanisms on left ventricular function in patients with dilated cardiomyopathy (358 views)
Eur J Heart Fail European Journal Of Heart Failure (ISSN: 1388-9842), 2002 Dec; 4(6): 727-735.
Impact Factor: 2.134
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Menchise V, Corbier C, Didierjean C, Saviano M, Benedetti E, Jacquot JP, Aubry A
* Crystal structure of the wild-type and D30A mutant thioredoxin h of Chlamydomonas reinhardtii and implications for the catalytic mechanism (798 views)
Biochem J (ISSN: 0264-6021, 1470-8728electronic, 0264-6021linking), 2001 Oct 1; 359(1): 65-75.
Impact Factor: 4.326
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Giacco R, Clemente G, Mancini M, D'Avanzo A, Mansueto G, Brighenti F, Lasorella G, Rivieccio AM, Rivellese AA, Riccardi G
Mechanisms Of The Hypoglycemic Effect Of Water Solubile Fiber In Non Insulin Dependent Diabetic Patients (309 views)
Amyloid, 1998 Dec; N/D: 1025-1025.
Impact Factor: 0
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Wink DA, Hanbauer I, Grisham MB, Laval F, Nims RW, Laval J, Cook J, Pacelli R, Liebmann J, Krishna M, Ford PC, Mitchell JB
Chemical biology of nitric oxide: Regulation and protective and toxic mechanisms (1124 views)
Current Topics In Cellular Regulation (ISSN: 0070-2137), 1996; 34: 159-187.
Impact Factor: 4.375
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35 Records (30 excluding Abstracts).
Total impact factor: 162.976 (139.64 excluding Abstracts).
Total 5 year impact factor: 148.756 (126.276 excluding Abstracts).
Total impact factor: 162.976 (139.64 excluding Abstracts).
Total 5 year impact factor: 148.756 (126.276 excluding Abstracts).
466 views. Last view on Saturday 21 September 2024, 8:54:41
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