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LIBRIS Formathandbok  (Information om MARC21)
FältnamnIndikatorerMetadata
00004405naa a2200397 4500
001oai:lup.lub.lu.se:8d1514dc-f9da-4d30-bc47-b588fd6671cb
003SwePub
008160401s2014 | |||||||||||000 ||eng|
0247 a https://lup.lub.lu.se/record/45282772 URI
0247 a https://doi.org/10.1073/pnas.14015641112 DOI
040 a (SwePub)lu
041 a engb eng
042 9 SwePub
072 7a art2 swepub-publicationtype
072 7a ref2 swepub-contenttype
1001 a Meisl, Georg4 aut
2451 0a Differences in nucleation behavior underlie the contrasting aggregation kinetics of the Aβ40 and Aβ42 peptides.
264 c 2014-06-17
264 1b Proceedings of the National Academy of Sciences,c 2014
520 a The two major forms of the amyloid-beta (Aβ) peptide found in plaques in patients suffering from Alzheimer's disease, Aβ40 and Aβ42, only differ by two amino acids in the C-terminal region, yet they display markedly different aggregation behavior. The origins of these differences have remained challenging to connect to specific molecular-level processes underlying the aggregation reaction. In this paper we use a general strategy to apply the conventional workflow of chemical kinetics to the aggregation of the Aβ40 peptide to identify the differences between Aβ40 and Aβ42 in terms of the microscopic determinants of the aggregation reaction. Our results reveal that the major source of aggregates in the case of Aβ40 is a fibril-catalyzed nucleation process, the multistep nature of which is evident through its saturation behavior. Moreover, our results show that the significant differences in the observed behavior of the two proteins originate not simply from a uniform increase in all microscopic rates for Aβ42 compared with Aβ40, but rather are due to a shift of more than one order of magnitude in the relative importance of primary nucleation versus fibril-catalyzed secondary nucleation processes. This analysis sheds light on the microscopic determinants of the aggregation behavior of the principal forms of Aβ and outlines a general approach toward achieving an understanding at the molecular level of the aberrant deposition of insoluble peptides in neurodegenerative disorders.
650 7a NATURVETENSKAPx Biologi0 (SwePub)1062 hsv//swe
650 7a NATURAL SCIENCESx Biological Sciences0 (SwePub)1062 hsv//eng
7001 a Yang, Xiaotingu Lund University,Lunds universitet,Biokemi och Strukturbiologi,Centrum för Molekylär Proteinvetenskap,Kemiska institutionen,Institutioner vid LTH,Lunds Tekniska Högskola,Biochemistry and Structural Biology,Center for Molecular Protein Science,Department of Chemistry,Departments at LTH,Faculty of Engineering, LTH4 aut0 (Swepub:lu)bioc-xiy
7001 a Hellstrand, Eriku Lund University,Lunds universitet,Kemiska institutionen,Institutioner vid LTH,Lunds Tekniska Högskola,Department of Chemistry,Departments at LTH,Faculty of Engineering, LTH4 aut0 (Swepub:lu)bpc-eht
7001 a Frohm, Birgittau Lund University,Lunds universitet,Biokemi och Strukturbiologi,Centrum för Molekylär Proteinvetenskap,Kemiska institutionen,Institutioner vid LTH,Lunds Tekniska Högskola,Biochemistry and Structural Biology,Center for Molecular Protein Science,Department of Chemistry,Departments at LTH,Faculty of Engineering, LTH4 aut0 (Swepub:lu)klke-bfr
7001 a Kirkegaard, Julius B4 aut
7001 a Cohen, Samuel I A4 aut
7001 a Dobson, Christopher M4 aut
7001 a Linse, Sarau Lund University,Lunds universitet,Biokemi och Strukturbiologi,Centrum för Molekylär Proteinvetenskap,Kemiska institutionen,Institutioner vid LTH,Lunds Tekniska Högskola,Biochemistry and Structural Biology,Center for Molecular Protein Science,Department of Chemistry,Departments at LTH,Faculty of Engineering, LTH4 aut0 (Swepub:lu)fkm2-sli
7001 a Knowles, Tuomas P J4 aut
7102 a Biokemi och Strukturbiologib Centrum för Molekylär Proteinvetenskap4 org
7730 t Proceedings of the National Academy of Sciencesd : Proceedings of the National Academy of Sciencesg 111:26, s. 9384-9389q 111:26<9384-9389x 1091-6490x 0027-8424
8564 u http://dx.doi.org/10.1073/pnas.1401564111y FULLTEXT
8564 u https://www.pnas.org/content/pnas/111/26/9384.full.pdf
8564 8u https://lup.lub.lu.se/record/4528277
8564 8u https://doi.org/10.1073/pnas.1401564111

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