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A peptide bond covalently attaches amino acids through a dehydration reaction. One amino acid's carboxyl group and another amino acid's amino group combine, releasing a water molecule. The resulting bond is the peptide bond. The products that such linkages form are peptides. As more amino acids join this growing chain, the resulting chain is a polypeptide. Each polypeptide has a free amino group at one end. This end has the N-terminal, or the amino-terminal, and the other end has a free...
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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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The cationic polymerization mechanism consists of three steps: initiation, propagation, and termination. In the initiation step of the polymerization process, the π bond of a monomer gets protonated by the Lewis acid catalyst, which is formed from boron trifluoride and water. The protonation of the π bond generates a carbocation stabilized by the electron‐donating group. In the propagation step, the π bond of the second monomer acts as a nucleophile and attacks the...
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The polymerization process that involves carbanion as an intermediate is called anionic polymerization. It is also a type of addition or chain-growth polymerization. Anionic polymerization gets initiated by a strong nucleophile such as an organolithium or a Grignard reagent. The most commonly used initiator for anionic polymerization is butyl lithium. Monomers involved in anionic polymerization must possess a vinyl group bonded to one or two electron-withdrawing groups. For instance,...
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Ion exchange chromatography separates charged molecules from a solution by reversibly exchanging them with mobile, or 'active', ions associated with the oppositely charged stationary phase. This method can be used to separate ions, soften and deionize water, and purify solutions. The polymers comprising the ion-exchange column are high-molecular-weight and chemically stable polymers, crosslinked to be porous and essentially insoluble. They are also functionalized with either acidic or...
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Anionic Chain-Growth Polymerization: Mechanism01:04

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The mechanism for anionic chain-growth polymerization involves initiation, propagation, and termination steps. In the initiation step, a nucleophilic anion, such as butyl lithium, initiates the polymerization process by attacking the π bond of the vinylic monomer. As a result, a carbanion, stabilized by the electron‐withdrawing group, is generated. The resulting carbanion acts as a Michael donor in the propagation step and attacks the second vinylic monomer, which acts as a Michael...
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Constructing Thioether/Vinyl Sulfide-tethered Helical Peptides Via Photo-induced Thiol-ene/yne Hydrothiolation
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Deciphering the Role of π-Interactions in Polyelectrolyte Complexes Using Rationally Designed Peptides.

Sara Tabandeh1, Cristina Elisabeth Lemus2, Lorraine Leon1,3

  • 1Department of Materials Science and Engineering, University of Central Florida, Orlando, FL 32816, USA.

Polymers
|July 2, 2021
PubMed
Summary
This summary is machine-generated.

Polypeptide sequences with π-interactions form stable complexes, not liquid condensates. Fluorine substitution disrupts these interactions, reducing stability and hydrogen bonding in these protein-mimetic structures.

Keywords:
chiralityphase separationpolyelectrolyte complexespolypeptidesself-assemblyπ-interactions

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Area of Science:

  • Biochemistry
  • Materials Science
  • Polymer Chemistry

Background:

  • Electrostatic and π-interactions are crucial for protein liquid-liquid phase separation and membraneless organelle formation.
  • Peptide sequence patterning offers a method to create protein-like structures with controlled chemical properties and interactions.

Purpose of the Study:

  • To investigate the role of π-interactions in the phase separation and secondary structure formation of polyelectrolyte complexes.
  • To explore how charge density and fluorine substitution on phenylalanine affect these interactions and complex properties.

Main Methods:

  • Design and synthesis of oppositely charged polypeptides incorporating phenylalanine, lysine, and glutamic acid.
  • Characterization using MALDI-TOF mass spectroscopy, 1H NMR, and circular dichroism (CD).
  • Analysis of secondary structures via FTIR spectroscopy and complex stability via critical salt concentration measurements. UV-vis spectroscopy was used for encapsulation studies.

Main Results:

  • Polyelectrolyte complexes formed solid precipitates, not liquid condensates, indicating strong inter-sequence interactions.
  • Secondary structures revealed hydrogen-bonded formations with a β-sheet signal.
  • Fluorine substitution reduced hydrogen bonding by inhibiting π-interactions.
  • π-interactions enhanced complex stability against salt, with higher critical salt concentrations observed for sequences with more phenylalanine residues.
  • Sequences with π-interactions and increased charge density efficiently encapsulated small molecules with π-bonds.

Conclusions:

  • The study highlights the complex interplay of ionic, hydrophobic, hydrogen bonding, and π-interactions in polyelectrolyte complex formation.
  • Findings enhance the understanding of phase separation phenomena in protein-mimetic systems.
  • π-interactions play a significant role in stabilizing polyelectrolyte complexes and influencing their structural properties.