Short Peptides as Inhibitors of Amyloid Aggregation

Bradley Neddenriep; Anastasia Calciano; Daniel Conti; Erin Sauve; Marissa Paterson; Edward Bruno; David A. Moffet

Short Peptides as Inhibitors of Amyloid Aggregation

Bradley Neddenriep, Anastasia Calciano, Daniel Conti, Erin Sauve, Marissa Paterson, Edward Bruno, David A. Moffet

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

Abstract

The misfolding and aggregation of proteins into amyloid has been linked to a variety of age-related diseases. Aggregation of proteins, such as Aβ in Alzheimer's disease and Islet Amyloid Polypeptide (IAPP, amylin) in type 2 diabetes, appears to lead to the formation of toxic assemblies. These assemblies range in size from small oligomers (2-8 proteins) to large fibrils (thousands of proteins). It remains unclear how these amyloidogenic proteins misfold and form toxic species, but growing evidence suggests that inhibiting the aggregation of these proteins could slow, if not prevent altogether, the progression of these diseases. We describe the use of small peptides (

Original language	English
Pages (from-to)	39-46
Journal	The open biotechnology journal
State	Published - Jan 1 2011

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http://digitalcommons.lmu.edu/chem-biochem_fac/6

Cite this

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title = "Short Peptides as Inhibitors of Amyloid Aggregation",

abstract = "The misfolding and aggregation of proteins into amyloid has been linked to a variety of age-related diseases. Aggregation of proteins, such as Aβ in Alzheimer's disease and Islet Amyloid Polypeptide (IAPP, amylin) in type 2 diabetes, appears to lead to the formation of toxic assemblies. These assemblies range in size from small oligomers (2-8 proteins) to large fibrils (thousands of proteins). It remains unclear how these amyloidogenic proteins misfold and form toxic species, but growing evidence suggests that inhibiting the aggregation of these proteins could slow, if not prevent altogether, the progression of these diseases. We describe the use of small peptides ( ",

author = "Bradley Neddenriep and Anastasia Calciano and Daniel Conti and Erin Sauve and Marissa Paterson and Edward Bruno and Moffet, \{David A.\}",

note = "Neddenriep B, Calciano A, Conti D, et al. Short Peptides as Inhibitors of Amyloid Aggregation. The open biotechnology journal. 2011;5:39-46. doi:10.2174/1874070701105010039.",

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T1 - Short Peptides as Inhibitors of Amyloid Aggregation

AU - Neddenriep, Bradley

AU - Calciano, Anastasia

AU - Conti, Daniel

AU - Sauve, Erin

AU - Paterson, Marissa

AU - Bruno, Edward

AU - Moffet, David A.

N1 - Neddenriep B, Calciano A, Conti D, et al. Short Peptides as Inhibitors of Amyloid Aggregation. The open biotechnology journal. 2011;5:39-46. doi:10.2174/1874070701105010039.

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Y1 - 2011/1/1

N2 - The misfolding and aggregation of proteins into amyloid has been linked to a variety of age-related diseases. Aggregation of proteins, such as Aβ in Alzheimer's disease and Islet Amyloid Polypeptide (IAPP, amylin) in type 2 diabetes, appears to lead to the formation of toxic assemblies. These assemblies range in size from small oligomers (2-8 proteins) to large fibrils (thousands of proteins). It remains unclear how these amyloidogenic proteins misfold and form toxic species, but growing evidence suggests that inhibiting the aggregation of these proteins could slow, if not prevent altogether, the progression of these diseases. We describe the use of small peptides (

AB - The misfolding and aggregation of proteins into amyloid has been linked to a variety of age-related diseases. Aggregation of proteins, such as Aβ in Alzheimer's disease and Islet Amyloid Polypeptide (IAPP, amylin) in type 2 diabetes, appears to lead to the formation of toxic assemblies. These assemblies range in size from small oligomers (2-8 proteins) to large fibrils (thousands of proteins). It remains unclear how these amyloidogenic proteins misfold and form toxic species, but growing evidence suggests that inhibiting the aggregation of these proteins could slow, if not prevent altogether, the progression of these diseases. We describe the use of small peptides (

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EP - 46

JO - The open biotechnology journal

JF - The open biotechnology journal

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