Journal
ACS OMEGA
Volume 7, Issue 44, Pages 39680-39689Publisher
AMER CHEMICAL SOC
DOI: 10.1021/acsomega.2c03360
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Funding
- Natural Science and Engineering Research Council of Canada (NSERC)
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Collagen IV networks are crucial for the structural integrity of an organism's tissues. Improper functioning of these networks has been associated with diseases. Sulfilimine cross-links play a critical role in forming and stabilizing these networks. The dynamic nature of sulfilimine bonds in collagen IV is crucial for network formation. Protonation influences protein structure stability and hydrogen bond interactions.
Collagen IV networks are an essential component of basement membranes that are important for their structural integrity and thus that of an organism's tissues. Improper functioning of these networks has been associated with several diseases. Cross-links, such as sulfilimine bonds interconnecting NC1 domains, are critical for forming and mechanically stabilizing these collagen IV networks. More specifically, the sulfilimine crosslinks form between methionine (Met93) and lysine/hydroxylsine (Lys211/Hyl211) residues of NC1 domains. Therefore, the dynamic nature of the sulfilimine bond in collagen IV is crucial for network formation. To understand the dynamic nature of a neutral and protonated sulfilimine bond in collagen IV, we performed molecular dynamics (MD) simulations on four sulfilimine showed that the neutral Met93S-NLys211 system has the smallest protein backbone and showed the cross-linked residues' RMSD value. The conformational change analyses showed that the conformations of the sulfilimine cross-linked residues take on a U-shape for the Met93S-NHyl211 and Met93S-HNHyl211+ systems, whereas the conformations of the sulfilimine cross-linked residues are more open for the Met93S-NLys211, and Met93S-NHLys211+ systems. Protonation is a crucial biochemical process to stabilize the protein structure or the biological cross-links. Furthermore, the protonation of the sulfilimine bond could potentially influence hydrogen bond interaction with near amino acid residues, and according to water distribution analyses, the sulfilimine bond can potentially exist in one or more protonation states.
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