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231224s2015 xx |||||o 00| ||eng c |
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|a 10.1021/acs.langmuir.5b02915
|2 doi
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|a pubmed24n0842.xml
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|a (DE-627)NLM252682009
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|a DE-627
|b ger
|c DE-627
|e rakwb
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|a eng
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|a Amyloidogenic Properties of Short α-L-Glutamic Acid Oligomers
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|c 2015
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|a Text
|b txt
|2 rdacontent
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|a ƒaComputermedien
|b c
|2 rdamedia
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|a ƒa Online-Ressource
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|a Date Completed 27.06.2016
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|a Date Revised 29.09.2015
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|a published: Print-Electronic
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|a Citation Status MEDLINE
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|a Poly-L-glutamic acid (PLGA) forms amyloid-like β2-fibrils with the main spectral component of vibrational amide I' band unusually shifted below 1600 cm(-1). This distinct infrared feature has been attributed to the presence of bifurcated hydrogen bonds coupling C═O and N-D (N-H) groups of the main chains to glutamate side chains. Here, we investigate how decreasing the chain length of PLGA affects its capacity to form β2-fibrils. A series of acidified aqueous solutions of synthetic (l-Glu)n peptides (n ≈ 200, 10, 6, 5, 4, and 3) were incubated at high temperature. We observed that n = 4 is the critical chain length for which formation of aggregates with the β2-like infrared features is still observed under such conditions. Interestingly, according to atomic force microscopy (AFM), the self-assembly of (L-Glu)n chains varying vastly in length produces fibrils with rather uniform diameters of approximately 4-6 nm. Kinetic experiments on (L-Glu)5 and (L-Glu)200 peptides indicate that the fibrillation is significantly accelerated not only in the presence of homologous seeds but also upon cross-seeding, suggesting thereby a common self-assembly theme for (L-Glu)n chains of various lengths. Our results are discussed in the context of mechanisms of amyloidogenic fibrillation of homopolypeptides
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|a Journal Article
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|a Research Support, Non-U.S. Gov't
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|a Amyloid
|2 NLM
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|a Polyglutamic Acid
|2 NLM
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|a 25513-46-6
|2 NLM
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|a Puławski, Wojciech
|e verfasserin
|4 aut
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|a Fedorczyk, Bartłomiej
|e verfasserin
|4 aut
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1 |
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|a Tymecka, Dagmara
|e verfasserin
|4 aut
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1 |
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|a Misicka, Aleksandra
|e verfasserin
|4 aut
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|a Filipek, Sławomir
|e verfasserin
|4 aut
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|a Dzwolak, Wojciech
|e verfasserin
|4 aut
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|i Enthalten in
|t Langmuir : the ACS journal of surfaces and colloids
|d 1999
|g 31(2015), 38 vom: 29. Sept., Seite 10500-7
|w (DE-627)NLM098181009
|x 1520-5827
|7 nnns
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|g volume:31
|g year:2015
|g number:38
|g day:29
|g month:09
|g pages:10500-7
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|u http://dx.doi.org/10.1021/acs.langmuir.5b02915
|3 Volltext
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|d 31
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