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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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Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
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Alkyl halides are halogen-substituted alkanes wherein one or more hydrogen atoms of an alkane is replaced by a halogen atom such as fluorine, chlorine, bromine, or iodine. The carbon atom in an alkyl halide is bonded to the halogen atom, which is sp3-hybridized and exhibits a tetrahedral shape.
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Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
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Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides
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Regulating Peptide Self-Assemblies by Halogen Bonding and Other Halogen Effects.

Anindyasundar Adak1,2, Payel Khanra1, Anindita Das1

  • 1School of Applied and Interdisciplinary Sciences, Indian Association for the Cultivation of Science (IACS), Jadavpur, Kolkata, INDIA.

Chemistry (Weinheim an Der Bergstrasse, Germany)
|February 19, 2026
PubMed
Summary

This study shows how halogen bonding and other halogen effects influence peptide self-assembly. Iodine-containing peptides exhibit greater stability and distinct self-assembly mechanisms compared to fluorinated analogues.

Keywords:
halogen bondinghydrogen bondingnanofiberpeptide assemblysupramolecular gel

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Area of Science:

  • Biomaterials Science
  • Supramolecular Chemistry
  • Chemical Biology

Background:

  • Peptide self-assembly is crucial for developing advanced biomaterials.
  • Understanding non-covalent interactions, like hydrogen bonding (HB) and halogen bonding (XB), is key to controlling self-assembly.
  • Halogen effects, beyond direct XB, can significantly impact molecular behavior.

Purpose of the Study:

  • To investigate the modulation of peptide self-assembly by halogen bonding (XB) and other halogen effects.
  • To compare the influence of iodine versus fluorine in functionalized peptides on self-assembly properties.
  • To elucidate the interplay between XB, HB, and hydrophobic interactions in peptide self-organization.

Main Methods:

  • Synthesis of three functionalized pentapeptides with a common FFK motif.
  • Incorporation of a tetrafluoroiodophenyl (TFIP) moiety as an XB donor.
  • Characterization of self-assembly, thermal stability, and viscoelastic properties using comprehensive studies.

Main Results:

  • Histidine-functionalized peptide showed significant C-I···N XB, while phenylalanine-terminated peptide showed negligible XB.
  • Iodine-containing peptides exhibited higher stability and enhanced viscoelastic properties than fluorinated analogues.
  • Distinct self-assembly mechanisms (cooperative vs. isodesmic) were observed, attributed to iodine's hydrophobicity and polarizability.

Conclusions:

  • Halogen bonding and other halogen effects, in synergy with hydrogen bonding, can modulate peptide self-assembly.
  • Iodine's unique properties lead to enhanced stability and different self-assembly behaviors compared to fluorine.
  • A delicate balance of XB, HB, and hydrophobic interactions fine-tunes peptide self-organization.