Calixarene docks dimethyllysine on lysozyme
p-Sulfonatocalix[4]arene selectively encapsulates Lys116-Me2 on dimethylated lysozyme, mimicking an aromatic cage.
Source
Structural study of a small molecule receptor bound to dimethyllysine in lysozyme
Study at a glance
- Design
- Other — Crystal and NMR study of p-sulfonatocalix[4]arene bound to dimethylated lysozyme lysines
- N
- Protein–small-molecule structural study — no cohort N
- Population
- Dimethylated hen egg-white lysozyme with sclx4
- Outcome
- Site-selective Lys-Me2 encapsulation by the calixarene
Structured fields used in claim comparison tables when every cited study has a complete layer.
What they did
Authors dimethylated hen lysozyme, solved sclx4 co-crystal structures, used 1H/13C NMR chemical shifts, and ran short MD at each Lys-Me2 site.
What they found
Lys116-Me2 is encapsulated in the calixarene; NMR shows a large upfield NεMe shift; accessibility and nearby Arg/Asn contacts explain selectivity versus other lysines.
The limits
What it doesn't show
No histone-tail co-crystal; MM-PBSA could not rank sites; precipitation limited solution stoichiometry.
Key terms
- Dimethyllysine (KMe2)
- Lysine post-translational methylation that creates a cation for aromatic-cage recognition.
- p-Sulfonatocalix[4]arene (sclx4)
- Anionic bowl-shaped receptor used as a synthetic lysine binder.
- Cation–π interaction
- Attraction between a cation (here NMe2) and aromatic faces of the calixarene.
- Aromatic cage
- Protein motif (e.g. chromodomain) that binds methyllysine with aromatics.
- Accessible surface area (ASA)
- Solvent-exposed area used to rank lysine steric accessibility.
Flashcards
Research intelligence for this paper
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Quiz yourself
Preferred dimethyllysine on lysozyme:
Common questions
Which lysine is selected?
Lys116-Me2, the most projecting dimethyllysine.
What NMR signature marks binding?
Large upfield shift of Lys116-Me2 NεMe at ~2.92 ppm.
What drives binding?
Cation–π plus hydrophobic cavity occupancy, not mainly salt bridges.
Why not other lysines?
Lower steric accessibility; MD shows Arg/Asn contacts unique to Lys116.
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