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Related Concept Videos

Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

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The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
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Intrinsically Disordered Proteins02:18

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Intrinsically disordered proteins are a group of proteins that do not fold into specific three-dimensional structures. Their structural flexibility allows them to complement ordered proteins to perform functions that are inaccessible to rigid structures. They are more common in eukaryotes than prokaryotes and may either be exclusively intrinsically disordered or hybrid proteins, consisting of a mix of ordered and disordered regions. The absence of a rigid structure in these proteins can be...
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Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a...
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Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
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Protein Networks02:26

Protein Networks

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An organism can have thousands of different proteins, and these proteins must cooperate to ensure the health of an organism. Proteins bind to other proteins and form complexes to carry out their functions. Many proteins interact with multiple other proteins creating a complex network of protein interactions.
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Imaging Protein-protein Interactions in vivo
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Inducing protein-protein interactions with molecular glues.

Ye Che1, Adam M Gilbert1, Veerabahu Shanmugasundaram1

  • 1Discovery Sciences, Medicine Design, Pfizer Worldwide Research and Development, Eastern Point Road, Groton, CT 06340, United States.

Bioorganic & Medicinal Chemistry Letters
|July 8, 2018
PubMed
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Discovering new therapeutic strategies, this study explores promoting novel protein-protein interactions to expand drug development beyond traditional binding sites. This approach offers a promising avenue for future drug interventions.

Keywords:
Induced protein interactionsMolecular gluesTargeted protein degradation

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Area of Science:

  • Medicinal Chemistry
  • Drug Discovery
  • Molecular Biology

Background:

  • The druggable proteome is constrained by the limited number of functional binding sites amenable to small molecule interaction and therapeutic response.
  • Orthosteric and allosteric modulation of enzymes and receptors are established drug action mechanisms.
  • Perturbing protein-protein interactions (PPIs) represents a newer, more challenging drug development strategy due to extensive contact surfaces.

Purpose of the Study:

  • To investigate the potential of small molecules that promote novel protein-protein interactions for therapeutic intervention.
  • To expand the scope of drug discovery beyond traditional binding site modulation.
  • To highlight precedents for PPI-promoting compounds in natural products and synthetic molecules.

Main Methods:

  • Literature review of established and emerging drug action mechanisms.
  • Analysis of the challenges and opportunities in targeting protein-protein interactions.
  • Examination of natural products and synthetic compounds that modulate PPIs.

Main Results:

  • Compounds promoting novel PPIs offer a significant expansion of therapeutic intervention opportunities.
  • Natural products like rapamycin and synthetic molecules such as thalidomide derivatives exemplify PPI modulation.
  • Targeting PPIs presents a difficult but potentially rewarding frontier in drug discovery.

Conclusions:

  • Promoting novel protein-protein interactions is a promising strategy to overcome limitations in the druggable proteome.
  • This approach broadens the landscape for small molecule therapeutics.
  • Further research into PPI-promoting compounds could lead to novel treatments.