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Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR

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Interaction of Atomically Precise Thiolated Copper Nanoclusters with Proteins: A Comparative Study.

Vinitha Packirisamy¹, Prabhu Pandurangan¹

¹Department of Physical Chemistry, School of Chemical Science, University of Madras, Guindy Campus, Chennai, Tamilnadu600 025, India.

|November 28, 2022

Summary

Glutathione-stabilized copper nanoclusters (CuNCs) were synthesized and characterized. These CuNCs showed minimal interaction with bovine serum albumin and lysozyme, indicating potential for biological applications.

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Generation of Scalable, Metallic High-Aspect Ratio Nanocomposites in a Biological Liquid Medium

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Area of Science:

Nanomaterials Science
Biochemistry
Spectroscopy

Background:

Copper nanoclusters (CuNCs) are emerging nanomaterials with unique photophysical properties.
Glutathione is a common capping agent for stabilizing metal nanoclusters.
Understanding protein-nanomaterial interactions is crucial for developing biocompatible nanoprobes.

Purpose of the Study:

To synthesize and characterize glutathione-stabilized copper nanoclusters (CuNCs).
To investigate the interaction of CuNCs with plasma proteins: bovine serum albumin (BSA), lysozyme (Lys), and hemoglobin (Hb).
To evaluate the potential of CuNCs for biological applications based on their protein interaction profiles.

Main Methods:

Facile synthesis of CuNCs in H2O/tetrahydrofuran medium.
Characterization using photophysical and morphological studies.
Electrospray ionization mass spectrometry for composition analysis (Cu12(SG)9).
Spectroscopic studies (UV-visible, fluorescence, circular dichroism) to analyze protein-CuNC interactions.

Main Results:

Synthesized CuNCs exhibited green emission, stability, and small size.
CuNCs showed minimal conformational changes and luminescence quenching with BSA and Lys due to weak interactions.
Significant changes in CuNC photophysical activity were observed with Hb, attributed to metallophic interactions.
Protein-CuNC interactions are influenced by functional groups on CuNCs and amino acid residues in proteins.

Conclusions:

Glutathione-stabilized CuNCs (Cu12(SG)9) are synthesized with desirable properties.
CuNCs demonstrate selective interaction profiles with plasma proteins.
Weak interactions with BSA and Lys suggest suitability for biological applications.
Strong interactions with Hb highlight the influence of metallophic binding and offer insights for targeted nanomedicine design.