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Amino Acids Trapped Inside C100: A Computational Study.

Satnam Singh1, Surajit Kayal2, Brijesh Kumar Mishra2

  • 1Department of Physical Sciences, Sant Baba Bhag Singh University, Jalandhar, Punjab, 144030, India.

Chemphyschem : a European Journal of Chemical Physics and Physical Chemistry
|December 21, 2025
PubMed
Summary
This summary is machine-generated.

The C100 fullerene effectively encapsulates amino acids like glycine, alanine, and serine, showing favorable interactions and stabilizing their structures. Encapsulation alters vibrational modes and reduces dipole moments, impacting their electronic properties.

Keywords:
amino acidsconfinementdipeptidesfullerene C100interaction energy

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Area of Science:

  • Computational Chemistry
  • Materials Science
  • Nanotechnology

Background:

  • Fullerenes, particularly C100, are explored for their potential as nanocontainers.
  • Amino acids are fundamental biological molecules with diverse properties.
  • Understanding host-guest interactions at the nanoscale is crucial for developing new materials.

Purpose of the Study:

  • To investigate the feasibility of using C100 fullerene as a nanocontainer for glycine, alanine, and serine.
  • To analyze the interaction energies and structural stability of encapsulated amino acids.
  • To examine the effects of encapsulation on amino acid vibrational modes, dipole moments, and NMR chemical shifts.

Main Methods:

  • Density Functional Theory (DFT) with B3LYP-D3 functional.
  • Second-order Møller-Plesset perturbation theory (MP2).
  • Domain-based local pair natural orbital-coupled cluster singles doubles and perturbative triples (DLPNO-CCSD(T)) method for high-accuracy calculations.

Main Results:

  • Calculated interaction energies indicate favorable host-guest interactions between C100 and the amino acids (-47.8 to -43.8 kcal/mol).
  • Encapsulation stabilizes both hydrogen-bonded and non-hydrogen-bonded conformers of the amino acids.
  • Vibrational analysis reveals restricted motion (blueshift) but strengthened hydrogen bonds (redshift in OH-stretch).
  • Significant reduction in dipole moments and downfield shifts in 1H NMR chemical shifts observed upon encapsulation.

Conclusions:

  • C100 fullerene is a feasible nanocontainer for small amino acids.
  • Encapsulation significantly modifies the electronic and vibrational properties of glycine, alanine, and serine.
  • The C100 cage effectively screens dipole moments and influences molecular dynamics.