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Updated: Sep 29, 2025

Studying Proteolysis of Cyclin B at the Single Cell Level in Whole Cell Populations

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Published on: September 17, 2012

The Study of Protein-Cyclitol Interactions.

Tetiana Dyrda-Terniuk^1,2, Mateusz Sugajski^1,2, Oleksandra Pryshchepa^1,2

¹Department of Environmental Chemistry and Bioanalytics, Faculty of Chemistry, Nicolaus Copernicus University in Toruń, Gagarina 7, 87-100 Toruń, Poland.

International Journal of Molecular Sciences

|March 25, 2022

Summary

This study explores how linear and cyclic cyclitols interact with Bovine Serum Albumin (BSA). The research reveals how cyclitol structure influences binding characteristics and molecular recognition mechanisms.

Keywords:

BSA bonding cyclitol interactions mechanism

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Cycloheximide Chase Analysis of Protein Degradation in Saccharomyces cerevisiae

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Published on: April 18, 2016

Area of Science:

Biochemistry
Molecular Biology
Structural Biology

Background:

Protein-ligand interactions are crucial for understanding molecular recognition and biological functions.
Bovine Serum Albumin (BSA) is a model protein frequently used to study drug binding and non-specific interactions.
Cyclitols, including linear (D-sorbitol, adonitol) and cyclic (shikimic acid, D-( )-quinic acid) forms, are investigated for their interaction profiles.

Purpose of the Study:

To investigate the non-specific interactions between Bovine Serum Albumin (BSA) and four distinct cyclitols.
To elucidate the impact of cyclitol structure (linear vs. cyclic) on the nature of protein-cyclitol interactions.
To understand the molecular recognition mechanisms governing these interactions.

Main Methods:

Chromatographic analysis (HPLC-MS/MS)
Electrophoretic analysis (SDS-PAGE)
Spectroscopic analysis (spectrofluorimetry, FTIR, Raman spectroscopy)
Isothermal Titration Calorimetry (ITC)
Computational modeling for binding site prediction
Kinetic studies for interaction mechanism elucidation

Main Results:

Detailed characterization of non-specific interactions between BSA and linear/cyclic cyclitols.
Identification of key structural features of cyclitols influencing binding affinity and mode.
Elucidation of interaction mechanisms through kinetic and thermodynamic analyses.
Validation of computational predictions for binding site identification.

Conclusions:

Cyclitol structure significantly impacts the character and mechanism of interaction with BSA.
The study provides insights into molecular recognition principles relevant to protein-ligand complexation.
Findings contribute to understanding cyclitol behavior in biological systems and potential therapeutic applications.