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Cisplatin Binding to Human Serum Transferrin: A Crystallographic Study.

Romualdo Troisi¹, Francesco Galardo¹, Giarita Ferraro¹

¹Department of Chemical Sciences, University of Naples Federico II, Complesso Universitario di Monte Sant'Angelo, via Cintia, Naples I-80126, Italy.

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|January 5, 2023

Summary

Human serum transferrin (hTF) binds the chemotherapy drug cisplatin at the atomic level. This interaction occurs at Met256 in the N-lobe without changing the protein

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Area of Science:

Biochemistry
Structural Biology
Pharmacology

Background:

The interaction between human serum transferrin (hTF) and platinum-based chemotherapy drugs like cisplatin is not fully understood at a molecular level.
Understanding this interaction is crucial for developing more effective cancer treatments and managing drug toxicity.

Purpose of the Study:

To elucidate the atomic-level molecular mechanism of how human serum transferrin (hTF) recognizes and binds to cisplatin.
To determine the structural consequences of cisplatin binding to hTF.

Main Methods:

X-ray crystallography or cryo-electron microscopy to determine the 3D structure of the hTF-cisplatin adduct.
Biochemical assays to confirm binding and assess functional impact.

Main Results:

The molecular structure of the adduct formed between hTF and cisplatin has been determined.
Cisplatin was found to bind to the side chain of methionine residue 256 (Met256) located in the N-lobe of hTF.
The binding of cisplatin to Met256 did not induce significant alterations in the overall conformation of the hTF protein.

Conclusions:

The study reveals the precise atomic interaction site of cisplatin with hTF.
This finding provides a structural basis for understanding how transferrin may influence cisplatin pharmacokinetics and efficacy.
The data offers insights for the rational design of platinum-based drugs or drug delivery systems involving transferrin.