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Amylin Derivative
The Experts below are selected from a list of 27 Experts worldwide ranked by ideXlab platform
Liskamp R.m.j. – One of the best experts on this subject based on the ideXlab platform.
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Inhibition of amyloid fibril formation of human Amylin by N-alkylated amino acid and -hydroxy acid residue containing peptides
, 2002Co-Authors: Rijkers D.t.s., Höppener J.w.m., Posthuma G., Lips C.j.m., Liskamp R.m.j.Abstract:Amyloid deposits are formed as a result of uncontrolled aggregation of (poly)peptides or proteins. Today several diseases are known, for example Alzheimer’s disease, Creutzfeldt–Jakob disease, mad cow disease, in which amyloid formation is involved. Amyloid fibrils are large aggregates of β-pleated sheets and here a general method is described to introduce molecular mutations in order to achieve disruption of β-sheet formation. Eight backbone-modified Amylin Derivatives, an amyloidogenic peptide involved in maturity onset diabetes, were synthesized. Their β-sheet forming properties were studied by IR spectroscopy and electron microscopy. Modification of a crucial amide NH by an alkyl chain led to a complete loss of the β-sheet forming capacity of Amylin. The resulting molecular mutated Amylin Derivative could be used to break the β-sheet thus retarding β-sheet formation of unmodified Amylin. Moreover, it was found that the replacement of this amide bond by an ester moiety suppressed fibrillogenesis significantly. Introduction of N-alkylated amino acids and/or ester functionalities—leading to depsipeptides—into amyloidogenic peptides opens new avenues towards novel peptidic β-sheet breakers for inhibition of β-amyloid aggregation
Rob M. J. Liskamp – One of the best experts on this subject based on the ideXlab platform.
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Inhibition of Amyloid Fibril Formation of Human Amylin by N-Alkylated Amino Acid and α-Hydroxy Acid Residue Containing Peptides
Chemistry – A European Journal, 2002Co-Authors: Dirk T. S. Rijkers, Jo W.m. Höppener, George Posthuma, Cornelis J.m. Lips, Rob M. J. LiskampAbstract:Amyloid deposits are formed as a result of uncontrolled aggregation of (poly)peptides or proteins. Today several diseases are known, for example Alzheimer’s disease, Creutzfeldt–Jakob disease, mad cow disease, in which amyloid formation is involved. Amyloid fibrils are large aggregates of β-pleated sheets and here a general method is described to introduce molecular mutations in order to achieve disruption of β-sheet formation. Eight backbone-modified Amylin Derivatives, an amyloidogenic peptide involved in maturity onset diabetes, were synthesized. Their β-sheet forming properties were studied by IR spectroscopy and electron microscopy. Modification of a crucial amide NH by an alkyl chain led to a complete loss of the β-sheet forming capacity of Amylin. The resulting molecular mutated Amylin Derivative could be used to break the β-sheet thus retarding β-sheet formation of unmodified Amylin. Moreover, it was found that the replacement of this amide bond by an ester moiety suppressed fibrillogenesis significantly. Introduction of N-alkylated amino acids and/or ester functionalities—leading to depsipeptides—into amyloidogenic peptides opens new avenues towards novel peptidic β-sheet breakers for inhibition of β-amyloid aggregation.
Rijkers D.t.s. – One of the best experts on this subject based on the ideXlab platform.
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Inhibition of amyloid fibril formation of human Amylin by N-alkylated amino acid and -hydroxy acid residue containing peptides
, 2002Co-Authors: Rijkers D.t.s., Höppener J.w.m., Posthuma G., Lips C.j.m., Liskamp R.m.j.Abstract:Amyloid deposits are formed as a result of uncontrolled aggregation of (poly)peptides or proteins. Today several diseases are known, for example Alzheimer’s disease, Creutzfeldt–Jakob disease, mad cow disease, in which amyloid formation is involved. Amyloid fibrils are large aggregates of β-pleated sheets and here a general method is described to introduce molecular mutations in order to achieve disruption of β-sheet formation. Eight backbone-modified Amylin Derivatives, an amyloidogenic peptide involved in maturity onset diabetes, were synthesized. Their β-sheet forming properties were studied by IR spectroscopy and electron microscopy. Modification of a crucial amide NH by an alkyl chain led to a complete loss of the β-sheet forming capacity of Amylin. The resulting molecular mutated Amylin Derivative could be used to break the β-sheet thus retarding β-sheet formation of unmodified Amylin. Moreover, it was found that the replacement of this amide bond by an ester moiety suppressed fibrillogenesis significantly. Introduction of N-alkylated amino acids and/or ester functionalities—leading to depsipeptides—into amyloidogenic peptides opens new avenues towards novel peptidic β-sheet breakers for inhibition of β-amyloid aggregation