publication . Doctoral thesis . 2012

Aggregation and toxicity of amyloid-beta peptide in relation to peptide sequence variation

A. Vandersteen;
Open Access English
  • Published: 12 Dec 2012
  • Publisher: Universiteit Twente
  • Country: Netherlands
Abstract
Generally, aggregation of the amyloid-s peptide is considered the cause of neuronal death in Alzheimer disease. The heterogenous As peptide occurs in various lengths in vivo: As40 and As42 are the predominant forms while both shorter and longer peptides exist. As40 and shorter isoforms are less aggregation-prone and hence considered less dangerous than As42 and longer isoforms, which are more aggregation-prone. Up to now research mainly focussed on the predominant As peptides and their individual characterization. This work emphasizes on the behavior of various isoforms in mixtures, as to mimick the in vivo situation. The results indicate that subtle differences...
Persistent Identifiers
Subjects
free text keywords: IR-81970, METIS-288677, In vivo, Amyloid beta, biology.protein, biology, Gene isoform, Biochemistry, Alzheimer's disease, medicine.disease, medicine, Amyloid, Peptide, chemistry.chemical_classification, chemistry, Toxicity, Peptide sequence
Related Organizations
63 references, page 1 of 5

[1] Lambert M, Barlow A, Chromy B, Edwards C, Freed R, Liosatos M, Morgan T, Rozovsky I, Trommer B, Viola K, Wals P, Zhang C, Finch C, Krafft G, Klein W (1998). Diffusible, nonfibrillar ligands derived from Aβ1-42 are potent central nervous system neurotoxins. Proc. Natl. Acad. Sci. USA, 95:6448- 6453.

[2] Hoyer W, Antony T, Cherny D, Heim G, Jovin T, Subramaniam V (2002). Dependence of α-synuclein aggregate morphology on solution conditions. J. Mol. Biol., 322:383-393.

[3] Bitan G, Kirkitadze M, Lomakin A, Vollers S, Benedek G, Teplow D (2003). Amyloid β-protein (Aβ) assembly: Aβ40 and Aβ42 oligomerize through distinct pathways. Proc. Natl. Acad. Sci. USA, 100:330-335. [OpenAIRE]

[4] Hepler R, Grimm K, Nahas D, Breese R, Dodson E, Acton P, Keller P, Yeager M, Wang H, Shugrue P, Kinney G, Joyce J (2006). Solution state characterization of amyloid β-derived diffusible ligands. Biochemistry, 45:15157-15167.

[5] Lesné S, Koh M, Kotilinek L, Kayed R, Glabe C, Yang A (2006). A specific amyloid-β protein assembly in the brain impairs memory. Nature, 440:352-357. [OpenAIRE]

[6] Jarrett J, Berger E, Lansbury P (1993). The carboxy terminus of the β amyloid protein is critical for the seeding of amyloid formation: implications for the pathogenesis of Alzheimer's disease. Biochem., 32:4693-4697. [OpenAIRE]

[7] Jarrett J & Lansbury P (1993). Seeding one-dimensional crystallization of amyloid: a pathogenic mechanism in Alzheimer's disease and scrapie? Cell, 73:1055-1058. [OpenAIRE]

[8] Snyder S, Ladror U, Wade W, Wang G, Barrett L, Matayoshi E, Huffaker H, Krafft G, Holzman T (1994). Amyloid-β aggregation: selective inhibition of aggregation in mixtures of amyloid with different chain lengths. Biophys. J., 67:1216-1228.

[9] Johansson A, Berglind-Dehlin F, Karlsson G, Edwards K, Gellerfors P, Lannfelt L (2006). Physiochemical characterization of the Alzheimer's disease-related peptides Aβ1-42 Arctic and Aβ1-42 wt. FEBS. J., 273:2618-2630.

[10] Kelly S, Jess T, Price N (2005). How to study proteins by circular dichroism. Biochim. Biophys. Acta, 1751:119-139.

[11] Loo J & Kaddis C (2007). Direct characterization of protein complexes by electrospray ionization mass spectrometry and ion mobility analysis. In: K Downard (2007). Mass spectrometry of Protein Interactions. Hoboken: Wiley & Sons, ch 1.

[12] Muskett F (2011). Sample preparation, data collection and processing. In: G Roberts & L-Y Lian eds. (2011). Protein NMR Spectroscopy: Practical techniques and applications. Hoboken: Wiley & Sons, ch 1.

[13] Burdick D, Soreghan B, Kwon M, Kosmoski J, Knauer M, Henschen A, Yates J, Cotman C, Glabe C (1992). Assembly and aggregation properties of synthetic Alzheimer's A4/β amyloid peptide analogs. J. Biol. Chem., 267:546-554.

[14] Harper J & Lansbury P (1997). Models of amyloid seeding in Alzheimer's disease and scrapie: Mechanistic truths and physiological consequences of the time-dependent solubility of amyloid proteins. Annu. Rev. Biochem., 66:385-407. [OpenAIRE]

[15] Bolognesi B, Kumita J, Barros T, Esbjorner E, Luheshi L, Crowther D, Wilson M, Dobson C, Favrin G, Yerbury J (2010). ANS binding reveals common features of cytotoxic amyloid species. ACS Chem. Biol., 5:735-740.

63 references, page 1 of 5
Abstract
Generally, aggregation of the amyloid-s peptide is considered the cause of neuronal death in Alzheimer disease. The heterogenous As peptide occurs in various lengths in vivo: As40 and As42 are the predominant forms while both shorter and longer peptides exist. As40 and shorter isoforms are less aggregation-prone and hence considered less dangerous than As42 and longer isoforms, which are more aggregation-prone. Up to now research mainly focussed on the predominant As peptides and their individual characterization. This work emphasizes on the behavior of various isoforms in mixtures, as to mimick the in vivo situation. The results indicate that subtle differences...
Persistent Identifiers
Subjects
free text keywords: IR-81970, METIS-288677, In vivo, Amyloid beta, biology.protein, biology, Gene isoform, Biochemistry, Alzheimer's disease, medicine.disease, medicine, Amyloid, Peptide, chemistry.chemical_classification, chemistry, Toxicity, Peptide sequence
Related Organizations
63 references, page 1 of 5

[1] Lambert M, Barlow A, Chromy B, Edwards C, Freed R, Liosatos M, Morgan T, Rozovsky I, Trommer B, Viola K, Wals P, Zhang C, Finch C, Krafft G, Klein W (1998). Diffusible, nonfibrillar ligands derived from Aβ1-42 are potent central nervous system neurotoxins. Proc. Natl. Acad. Sci. USA, 95:6448- 6453.

[2] Hoyer W, Antony T, Cherny D, Heim G, Jovin T, Subramaniam V (2002). Dependence of α-synuclein aggregate morphology on solution conditions. J. Mol. Biol., 322:383-393.

[3] Bitan G, Kirkitadze M, Lomakin A, Vollers S, Benedek G, Teplow D (2003). Amyloid β-protein (Aβ) assembly: Aβ40 and Aβ42 oligomerize through distinct pathways. Proc. Natl. Acad. Sci. USA, 100:330-335. [OpenAIRE]

[4] Hepler R, Grimm K, Nahas D, Breese R, Dodson E, Acton P, Keller P, Yeager M, Wang H, Shugrue P, Kinney G, Joyce J (2006). Solution state characterization of amyloid β-derived diffusible ligands. Biochemistry, 45:15157-15167.

[5] Lesné S, Koh M, Kotilinek L, Kayed R, Glabe C, Yang A (2006). A specific amyloid-β protein assembly in the brain impairs memory. Nature, 440:352-357. [OpenAIRE]

[6] Jarrett J, Berger E, Lansbury P (1993). The carboxy terminus of the β amyloid protein is critical for the seeding of amyloid formation: implications for the pathogenesis of Alzheimer's disease. Biochem., 32:4693-4697. [OpenAIRE]

[7] Jarrett J & Lansbury P (1993). Seeding one-dimensional crystallization of amyloid: a pathogenic mechanism in Alzheimer's disease and scrapie? Cell, 73:1055-1058. [OpenAIRE]

[8] Snyder S, Ladror U, Wade W, Wang G, Barrett L, Matayoshi E, Huffaker H, Krafft G, Holzman T (1994). Amyloid-β aggregation: selective inhibition of aggregation in mixtures of amyloid with different chain lengths. Biophys. J., 67:1216-1228.

[9] Johansson A, Berglind-Dehlin F, Karlsson G, Edwards K, Gellerfors P, Lannfelt L (2006). Physiochemical characterization of the Alzheimer's disease-related peptides Aβ1-42 Arctic and Aβ1-42 wt. FEBS. J., 273:2618-2630.

[10] Kelly S, Jess T, Price N (2005). How to study proteins by circular dichroism. Biochim. Biophys. Acta, 1751:119-139.

[11] Loo J & Kaddis C (2007). Direct characterization of protein complexes by electrospray ionization mass spectrometry and ion mobility analysis. In: K Downard (2007). Mass spectrometry of Protein Interactions. Hoboken: Wiley & Sons, ch 1.

[12] Muskett F (2011). Sample preparation, data collection and processing. In: G Roberts & L-Y Lian eds. (2011). Protein NMR Spectroscopy: Practical techniques and applications. Hoboken: Wiley & Sons, ch 1.

[13] Burdick D, Soreghan B, Kwon M, Kosmoski J, Knauer M, Henschen A, Yates J, Cotman C, Glabe C (1992). Assembly and aggregation properties of synthetic Alzheimer's A4/β amyloid peptide analogs. J. Biol. Chem., 267:546-554.

[14] Harper J & Lansbury P (1997). Models of amyloid seeding in Alzheimer's disease and scrapie: Mechanistic truths and physiological consequences of the time-dependent solubility of amyloid proteins. Annu. Rev. Biochem., 66:385-407. [OpenAIRE]

[15] Bolognesi B, Kumita J, Barros T, Esbjorner E, Luheshi L, Crowther D, Wilson M, Dobson C, Favrin G, Yerbury J (2010). ANS binding reveals common features of cytotoxic amyloid species. ACS Chem. Biol., 5:735-740.

63 references, page 1 of 5
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