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Interaction between astaxanthin and the glutamic acid (GLU 124) residue at the bacterial protein binding interface, as captured by molecular dynamics simulation. This residue contact contributes to the overall binding affinity.

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![Figure 71: Interaction between astaxanthin and the glutamic acid (GLU 124) residue at the bacterial protein binding interface, as captured by molecular dynamics simulation. This residue contact contributes to the overall binding affinity.]()

> Source: Jamiu Olaseni Aribisala et al. "Astaxanthin-Mediated Bacterial Lethality: Evidence from Oxidative Stress Contrib." *Oxidative medicine and cellular longevity*, 2021. PMID: [34925700](https://pubmed.ncbi.nlm.nih.gov/34925700/)
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  <img src="" alt="Interaction between astaxanthin and the glutamic acid (GLU 124) residue at the bacterial protein binding interface, as captured by molecular dynamics simulation. This residue contact contributes to the overall binding affinity." />
  <figcaption>Figure 71. Interaction between astaxanthin and the glutamic acid (GLU 124) residue at the bacterial protein binding interface, as captured by molecular dynamics simulation. This residue contact contributes to the overall binding affinity.<br>  Source: Jamiu Olaseni Aribisala et al. "Astaxanthin-Mediated Bacterial Lethality: Evidence from Oxidative Stress Contrib." <em>Oxidative medicine and cellular longevity</em>, 2021. PMID: <a href="https://pubmed.ncbi.nlm.nih.gov/34925700/">34925700</a></figcaption>
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