Phage display affords peptides that modulate beta-amyloid aggregation.

Phage display affords peptides that modulate beta-amyloid aggregation. Research Abstract Details 

Research Abstract Table of Contents

Jump to the:

Phage display affords peptides that modulate beta-amyloid aggregation. Abstract Text:

Brendan P Orner,Lin Liu,Regina M Murphy,Laura L Kiessling,

As the population ages, the need to develop methods to understand and intercept the processes responsible for protein aggregation diseases is becoming more urgent. The aggregation of the protein beta-amyloid (Abeta) has been implicated in Alzheimer's Disease (AD); however, whether the toxic species is a large, insoluble aggregate or some lower order form is not yet known. Agents that can modulate the aggregation state of Abeta could resolve this controversy by facilitating our understanding of the consequences of aggregation and its underlying mechanism. To date, however, ligands that bind to specific forms of Abeta have not been identified. To address this deficiency, we tested whether phage display could yield such ligands by screening libraries against Abeta in two different states: monomeric or highly aggregated. Intriguingly, the peptides selected had different effects on Abeta aggregation. Peptides selected for binding to monomeric Abeta did not perturb aggregation, but those selected using highly aggregated Abeta increase the rate of aggregation drastically. The latter also alter the morphology of the resulting aggregate. The ability of a peptide to promote aggregation correlated with its affinity for the N-terminal 10 residues of Abeta. This result indicates that the mechanism by which the peptides influence aggregation is related to their affinity for the Abeta N-terminus. Thus, the identification of compounds that bind to this Abeta section can afford agents that affect aggregation. Moreover, the data suggest that endogenous ligands that interact with the N-terminal region can influence the propensity of Abeta to form aggregates and the morphology of those that form. Our data highlight the utility of phage display for identifying ligands that bind to target proteins in different states, and they indicate that such agents can be used to perturb protein aggregation.

Phage display affords peptides that modulate beta-amyloid aggregation. Publishing Authors By Initials

BP Orner,L Liu,RM Murphy,LL Kiessling,

For similar abstracts research abstracts see: abstracts research

PUBMED ID PMID:

MEDLINE DATE:

Phage display affords peptides that modulate beta-amyloid aggregation. Journal Published:

PUBLICATION TYPE: Research Support, U.S. Gov't,

Journal: Journal of the American Chemical Society

VOLUME: 128

Page Numbers: 11882-9

Journal Abbreviation:

ISSN: 0002-7863

DAY: 13

MONTH: Sep

YEAR: 2006

Phage display affords peptides that modulate beta-amyloid aggregation. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 7503056

Phage display affords peptides that modulate beta-amyloid aggregation. Keywords Mesh Terms:

KEYWORDS:

MESH TERMS:

Chemical & Substance for Abstract: Phage display affords peptides that modulate beta-amyloid aggregation. Information

Substance Name:

Registry Number:

Grant and Affiliation Information for Phage display affords peptides that modulate beta-amyloid aggregation.

AFFILIATION: Department of Biochemistry, University of Wisconsin-Madison, Madison, Wisconsin 53706, USA.

Country: United States

AGENCY:

GRANT:

ACRONYM:

MEDLINETA: J Am Chem Soc

REFSOURCE:

DATABASENAME:

ACCESSION NUMBER:

Number Hits: 0

Phage display affords peptides that modulate beta-amyloid aggregation Related Publications

• A method for preparing boron of high purity.
• A polymer scaffold for protein oligomerization.
• A polymeric domain that promotes cellular internalization.
• A possible localization of -glycerophosphate dehydrogenase to the inner boundary membrane of mitochondria in livers from rats fed with ethanol.
• Activating B cell signaling with defined multivalent ligands.
• Arrays for the combinatorial exploration of cell adhesion.
• Bifunctional ligands that target cells displaying the alpha v beta3 integrin.
• Chemical probes of UDP-galactopyranose mutase.
• Contrast agents for magnetic resonance imaging synthesized with ring-opening metathesis polymerization.
• Defined substrates for human embryonic stem cell growth identified from surface arrays.
• Endogenous retrovirus expression in testis and epididymis.
• Human embryonic stem cells: the practical handbook.
• Identification of inhibitors for UDP-galactopyranose mutase.
• Inhibitors of UDP-galactopyranose mutase thwart mycobacterial growth.
• Molecular profiling of angiogenesis with targeted ultrasound imaging: early assessment of antiangiogenic therapy effects.
• N-acylsulfonamide linker activation by Pd-catalyzed allylation.
• Non-carbohydrate inhibitors of the lectin DC-SIGN.
• Phage display affords peptides that modulate beta-amyloid aggregation.
• Pharmacodynamics of streptavidin-coated cyanoacrylate microbubbles designed for molecular ultrasound imaging.
• Rabson-Mendenhall syndrome: medullary sponge kidney, a new component.
• Retrospective motion gating in small animal CT of mice and rats.
• Selective tumor cell targeting using low-affinity, multivalent interactions.
• Solid-phase synthesis of alkanethiols for the preparation of self-assembled monolayers.
• Solid-phase synthesis of polymers using the ring-opening metathesis polymerization.
• The CD16- CD56(bright) NK cell subset is resistant to reactive oxygen species produced by activated granulocytes and has higher antioxidative capacity than the CD16+ CD56(dim) subset.
• The effect of insulin on the synthesis and dephosphorylation of thiamine diphosphate in liver homogenates from alloxan diabetic rats.
• Volumetric high-frequency Doppler ultrasound enables the assessment of early antiangiogenic therapy effects on tumor xenografts in nude mice.
• [Andrologic problems in general practive]
• [Clinical and experimental studies with azulene-containing ointments and solutions in dermatology.]
• [Clinical results with internal and intramuscular administration of biotin.]