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A competitive low-affinity binding model for determining the mutual and specific sites of two ligands on protein.

Author: BaiGuoyun, CuiYanfang, LiuMaili, YangYunhuang, YeChaohui

Journal ArticleAn article published in an academic or professional journal that reports original research or scholarly analysis.
Research Support, Non-U.S. Gov'tResearch funding provided by government agencies outside the United States.

Overview

A competitive low-affinity binding model was proposed to determine the number of mutual and specific binding sites of two ligands on a protein. The model was examined using human serum albumin (HSA) as a receptor and tolmetin (TOL) and salicylic acid (SAL) as ligands. It was found that HSA has a large binding capacity for most ligands, but there are still a reasonable amount of the low-affinity binding sites that are structure selective.
Paper Details　
Original Abstract of the Article :
A competitive low-affinity binding model was proposed for determining the number of mutual (overlapped) and specific binding sites of two ligands (A, B) on a protein (P). To use the model, one needs to carry out a titration experiment by adding either ligand A or B into a three-component system (A-B...See full text at original site
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引用元：
https://doi.org/10.1016/j.jpba.2004.12.037

データ提供：米国国立医学図書館（NLM）

Competitive Low-Affinity Binding Model for Ligand Interactions

This study introduces a new model for determining the mutual and specific binding sites of two ligands on a protein. The researchers developed a competitive low-affinity binding model, which utilizes titration experiments to monitor the spectroscopic parameter changes as ligands are added to a protein solution.

Understanding Ligand Binding Sites

The study successfully applied the proposed model to human serum albumin (HSA), using tolmetin (TOL) and salicylic acid (SAL) as ligands. By analyzing the titration data, the researchers identified the mutual and specific binding sites of the two ligands on HSA. This model offers a valuable tool for understanding the complex interactions between ligands and proteins.

Impact on Drug Discovery and Development

The insights gained from this research contribute to a better understanding of ligand-protein interactions, which is crucial for drug discovery and development. By elucidating the binding mechanisms of different ligands, this study provides valuable information for designing more effective and targeted drugs that can bind specifically to their intended targets.

Dr.Camel's Conclusion

This research, like a desert explorer uncovering a hidden oasis, provides a novel model for analyzing the intricate interactions between ligands and proteins. The study's findings offer a valuable tool for understanding ligand binding sites, potentially advancing drug discovery and development by enabling the design of more targeted and effective therapies.

Date :
  1. Date Completed 2005-09-19
  2. Date Revised 2017-11-16
Further Info :

Pubmed ID

15967285

DOI: Digital Object Identifier

10.1016/j.jpba.2004.12.037

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in preparation
Languages

English

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