Influence of heparin and dendrimers on the aggregation of two amyloid peptides related to Alzheimer's and prion diseases

Barbara Klajnert; Marta Cortijo-Arellano; Maria Bryszewska; Josep Cladera

doi:10.1016/j.bbrc.2005.11.053

Influence of heparin and dendrimers on the aggregation of two amyloid peptides related to Alzheimer's and prion diseases

Barbara Klajnert, Marta Cortijo-Arellano, Maria Bryszewska, Josep Cladera^*

^*Corresponding author for this work

Research output: Contribution to journal › Article › Research › peer-review

101 Citations (Scopus)

Abstract

Amyloid plaques composed of proteinaceous aggregates are commonly found in brains affected by Alzheimer's disease and spongiform encephalopaties. A structural homology has been recently described for the Alzheimer's peptide Aβ1-28 and the segment of the prion protein Prp185-208. In the present paper, further elements in common are reported: the aggregation processes are in both cases enhanced by the model glucosaminoglycan heparin and dendrimers can modulate the aggregation process by affecting the nucleation rate at low concentrations and the elongation rate at high concentrations. Nucleation and elongation rate constants are derived from fittings to a nucleation dependent polymerization model. © 2005 Elsevier Inc. All rights reserved.

Original language	English
Pages (from-to)	577-582
Journal	Biochemical and Biophysical Research Communications
Volume	339
Issue number	2
DOIs	https://doi.org/10.1016/j.bbrc.2005.11.053
Publication status	Published - 13 Jan 2006

Keywords

Alzheimer
Amyloid
Dendrimer
Heparin
Prion

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10.1016/j.bbrc.2005.11.053

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title = "Influence of heparin and dendrimers on the aggregation of two amyloid peptides related to Alzheimer's and prion diseases",

abstract = "Amyloid plaques composed of proteinaceous aggregates are commonly found in brains affected by Alzheimer's disease and spongiform encephalopaties. A structural homology has been recently described for the Alzheimer's peptide Aβ1-28 and the segment of the prion protein Prp185-208. In the present paper, further elements in common are reported: the aggregation processes are in both cases enhanced by the model glucosaminoglycan heparin and dendrimers can modulate the aggregation process by affecting the nucleation rate at low concentrations and the elongation rate at high concentrations. Nucleation and elongation rate constants are derived from fittings to a nucleation dependent polymerization model. {\textcopyright} 2005 Elsevier Inc. All rights reserved.",

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Influence of heparin and dendrimers on the aggregation of two amyloid peptides related to Alzheimer's and prion diseases. / Klajnert, Barbara; Cortijo-Arellano, Marta; Bryszewska, Maria et al.

In: Biochemical and Biophysical Research Communications, Vol. 339, No. 2, 13.01.2006, p. 577-582.

Research output: Contribution to journal › Article › Research › peer-review

TY - JOUR

T1 - Influence of heparin and dendrimers on the aggregation of two amyloid peptides related to Alzheimer's and prion diseases

AU - Klajnert, Barbara

AU - Cortijo-Arellano, Marta

AU - Bryszewska, Maria

AU - Cladera, Josep

PY - 2006/1/13

Y1 - 2006/1/13

N2 - Amyloid plaques composed of proteinaceous aggregates are commonly found in brains affected by Alzheimer's disease and spongiform encephalopaties. A structural homology has been recently described for the Alzheimer's peptide Aβ1-28 and the segment of the prion protein Prp185-208. In the present paper, further elements in common are reported: the aggregation processes are in both cases enhanced by the model glucosaminoglycan heparin and dendrimers can modulate the aggregation process by affecting the nucleation rate at low concentrations and the elongation rate at high concentrations. Nucleation and elongation rate constants are derived from fittings to a nucleation dependent polymerization model. © 2005 Elsevier Inc. All rights reserved.

AB - Amyloid plaques composed of proteinaceous aggregates are commonly found in brains affected by Alzheimer's disease and spongiform encephalopaties. A structural homology has been recently described for the Alzheimer's peptide Aβ1-28 and the segment of the prion protein Prp185-208. In the present paper, further elements in common are reported: the aggregation processes are in both cases enhanced by the model glucosaminoglycan heparin and dendrimers can modulate the aggregation process by affecting the nucleation rate at low concentrations and the elongation rate at high concentrations. Nucleation and elongation rate constants are derived from fittings to a nucleation dependent polymerization model. © 2005 Elsevier Inc. All rights reserved.

KW - Alzheimer

KW - Amyloid

KW - Dendrimer

KW - Heparin

KW - Prion

U2 - 10.1016/j.bbrc.2005.11.053

DO - 10.1016/j.bbrc.2005.11.053

M3 - Article

SN - 0006-291X

VL - 339

SP - 577

EP - 582

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

IS - 2

ER -

Influence of heparin and dendrimers on the aggregation of two amyloid peptides related to Alzheimer's and prion diseases

Abstract

Keywords

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