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Related Concept Videos

Chirality in Nature02:30

Chirality in Nature

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Chirality is the most intriguing yet essential facet of nature, governing life’s biochemical processes and precision. It can be observed from a snail shell pattern in a macroscopic world to an amino acid, the minutest building block of life. Most of the snails around the world have right-coiled shells because of the intrinsic chirality in their genes. All the amino acids present in the human body exist in an enantiomerically pure state, except for glycine - the sole achiral amino acid.
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Amyloid Fibrils03:03

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Amyloid fibrils are aggregates of misfolded proteins.  Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils. 
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Chirality02:25

Chirality

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Chirality is a term that describes the lack of mirror symmetry in an object. In other words, chiral objects cannot be superposed on their mirror images. For example, our feet are chiral, as the mirror image of the left foot, the right foot, cannot be superposed on the left foot.
Chiral objects exhibit a sense of handedness when they interact with another chiral object. For example, our left foot can only fit in the left shoe and not in the right shoe. Achiral objects — objects that have...
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Prochirality02:05

Prochirality

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The concept of prochirality leads to the nomenclature of the individual faces of a molecule and plays a crucial role in the enantioselective reaction. It is a concept where two or more achiral molecules react to produce chiral products. A typical process is the reaction of an achiral ketone to generate a chiral alcohol. Here, the achiral reactant reacts with an achiral reducing agent, sodium borohydride, to generate an equimolar mixture of the chiral enantiomers of the product. For example, an...
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Molecules that possess multiple chiral centers can afford a large number of stereoisomers. For instance, while some molecules like 2-butanol have one chiral center, defined as a tetrahedral carbon atom with four different substituents attached, several molecules like butane-2,3-diol have multiple chiral centers. A simple formula to predict the number of stereoisomers possible for a molecule with n chiral centers is 2n. However, there can be a lower number where some of the stereoisomers are...
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A11-positive β-amyloid Oligomer Preparation and Assessment Using Dot Blotting Analysis
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Understanding and controlling amyloid aggregation with chirality.

Alejandro R Foley1, Jevgenij A Raskatov1

  • 1Department of Chemistry and Biochemistry, University of California Santa Cruz, Santa Cruz, CA, 95064, USA.

Current Opinion in Chemical Biology
|February 21, 2021
PubMed
Summary
This summary is machine-generated.

Chiral modifications, like using mirror-image peptides and D-amino acids, offer new ways to control amyloid aggregation. This research provides insights into disease mechanisms and identifies key sequences influencing amyloid fibril growth and toxicity.

Keywords:
AmyloidChiralityMirror-image peptidesModulation of aggregation pathways

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Neuroscience

Background:

  • Amyloid aggregation is linked to human diseases such as Alzheimer's, Parkinson's, and type II diabetes.
  • Despite advances, controlling amyloid fibril formation remains a significant research challenge.

Purpose of the Study:

  • To summarize recent advances in using chiral modifications to modulate amyloid aggregation.
  • To explore how mirror-image peptides and D-amino acids provide new mechanistic tools and insights into amyloidogenic processes.

Main Methods:

  • Utilizing mirror-image peptides and proteins.
  • Incorporating D-amino acids into peptide sequences.
  • Analyzing modulation of amyloid aggregation pathways.

Main Results:

  • Chiral modifications provide access to novel aggregation pathways.
  • Mirror-image peptides and D-amino acids modulate amyloid aggregation.
  • Key sequence positions influencing fibril growth and toxicity were identified.

Conclusions:

  • Chiral modifications are a promising strategy for controlling amyloid aggregation.
  • This approach offers new tools for studying cellular interactions and disease mechanisms.
  • Understanding sequence-dependent influences is crucial for therapeutic development.