{"title":"Investigating the binding dynamics and stability of bovine serum albumin with antibiotics with acridinedione dye.","authors":"Keerthiga Ravichandran, Rithika Kumaran, Kumaran Rajendran, Shoba Gunasekaran, Dhenadhayalan Namasivayam, Krishnan Anju","doi":"10.1016/j.pharma.2025.01.006","DOIUrl":null,"url":null,"abstract":"<p><p>Exploring the energetics and bimolecular interaction of bovine serum albumin (BSA) with various classes and generations of antibiotics in the absence and presence of a resorcinol based acridinedione dye (ADR1) were carried out. The binding stability of BSA-antibiotic complexes decreases on the introduction of ADR1 dye resulting in a positive value of free energy change, accompanied with several unfavourable interactions. Several polar amino acids contributed to the stability of the host-guest complex compared to that of non-polar amino acids, wherein BSA acts as the host, and antibiotics as the guest and ADR1 dye as the competing guest molecule. Hydrogen-bonding interactions govern the binding stability and energetics compared to that of hydrophobic interactions is elucidated in the present study.</p>","PeriodicalId":8332,"journal":{"name":"Annales pharmaceutiques francaises","volume":" ","pages":""},"PeriodicalIF":1.0000,"publicationDate":"2025-01-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Annales pharmaceutiques francaises","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1016/j.pharma.2025.01.006","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q4","JCRName":"PHARMACOLOGY & PHARMACY","Score":null,"Total":0}
引用次数: 0
Abstract
Exploring the energetics and bimolecular interaction of bovine serum albumin (BSA) with various classes and generations of antibiotics in the absence and presence of a resorcinol based acridinedione dye (ADR1) were carried out. The binding stability of BSA-antibiotic complexes decreases on the introduction of ADR1 dye resulting in a positive value of free energy change, accompanied with several unfavourable interactions. Several polar amino acids contributed to the stability of the host-guest complex compared to that of non-polar amino acids, wherein BSA acts as the host, and antibiotics as the guest and ADR1 dye as the competing guest molecule. Hydrogen-bonding interactions govern the binding stability and energetics compared to that of hydrophobic interactions is elucidated in the present study.
期刊介绍：
This journal proposes a scientific information validated and indexed to be informed about the last research works in all the domains interesting the pharmacy. The original works, general reviews, the focusing, the brief notes, subjected by the best academics and the professionals, propose a synthetic approach of the last progress accomplished in the concerned sectors. The thematic Sessions and the – life of the Academy – resume the communications which, presented in front of the national Academy of pharmacy, are in the heart of the current events.
京公网安备 11010802042870号
京ICP备2023020795号-1
分享
求助内容：
应助结果提醒方式：
扫码关注我们
