Amit G. Rathod , Priyanka Tiwari , Jatin Shaily, Sanjay Tiwari
{"title":"槲皮素对模型蛋白牛血清白蛋白的稳定作用","authors":"Amit G. Rathod , Priyanka Tiwari , Jatin Shaily, Sanjay Tiwari","doi":"10.1016/j.colsurfb.2025.114663","DOIUrl":null,"url":null,"abstract":"<div><div>Quercetin (QCT), an emerging class of flavonoid known for antioxidant and anti-inflammatory activities, has been studied for its protein stabilizing effect. After demonstrating ethanol (EtOH) - induced structural changes in bovine serum albumin (BSA), the stabilizing effect of QCT was studied using fluorescence, circular dichroism (CD) and Fourier transform infrared (FTIR) spectroscopic techniques. Morphological changes were examined using atomic force microscopy (AFM). EtOH triggered blue shift in fluorescence spectra of BSA and its intensity increased at higher percentage of alcohol. A reversal in this trend was recorded in the presence of QCT. This was interpreted as anti-amyloidogenic effect emanating from the binding of QCT to hydrophobic pockets of BSA. The value of binding constant (1.25 x 10<sup>6</sup> M<sup>−1</sup>; 298 K) is suggestive of strong binding affinity of QCT for BSA. The mode of QCT-induced fluorescence quenching was found to be mixed in nature. CD spectra showed that the protein conformation was altered and traces of alpha helix disappeared in the presence of EtOH. Contrarily, disruptive effect of EtOH was not visible upon incorporating QCT. This was further verifiable form the thermal CD data, which showed an upshift in the denaturation temperature of BSA. The data of thioflavin T assay and AFM further substantiated the protective effect of QCT.</div></div>","PeriodicalId":279,"journal":{"name":"Colloids and Surfaces B: Biointerfaces","volume":"252 ","pages":"Article 114663"},"PeriodicalIF":5.4000,"publicationDate":"2025-03-28","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Stabilizing effect of quercetin upon bovine serum albumin as a model protein\",\"authors\":\"Amit G. Rathod , Priyanka Tiwari , Jatin Shaily, Sanjay Tiwari\",\"doi\":\"10.1016/j.colsurfb.2025.114663\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><div>Quercetin (QCT), an emerging class of flavonoid known for antioxidant and anti-inflammatory activities, has been studied for its protein stabilizing effect. After demonstrating ethanol (EtOH) - induced structural changes in bovine serum albumin (BSA), the stabilizing effect of QCT was studied using fluorescence, circular dichroism (CD) and Fourier transform infrared (FTIR) spectroscopic techniques. Morphological changes were examined using atomic force microscopy (AFM). EtOH triggered blue shift in fluorescence spectra of BSA and its intensity increased at higher percentage of alcohol. A reversal in this trend was recorded in the presence of QCT. This was interpreted as anti-amyloidogenic effect emanating from the binding of QCT to hydrophobic pockets of BSA. The value of binding constant (1.25 x 10<sup>6</sup> M<sup>−1</sup>; 298 K) is suggestive of strong binding affinity of QCT for BSA. The mode of QCT-induced fluorescence quenching was found to be mixed in nature. CD spectra showed that the protein conformation was altered and traces of alpha helix disappeared in the presence of EtOH. Contrarily, disruptive effect of EtOH was not visible upon incorporating QCT. This was further verifiable form the thermal CD data, which showed an upshift in the denaturation temperature of BSA. The data of thioflavin T assay and AFM further substantiated the protective effect of QCT.</div></div>\",\"PeriodicalId\":279,\"journal\":{\"name\":\"Colloids and Surfaces B: Biointerfaces\",\"volume\":\"252 \",\"pages\":\"Article 114663\"},\"PeriodicalIF\":5.4000,\"publicationDate\":\"2025-03-28\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Colloids and Surfaces B: Biointerfaces\",\"FirstCategoryId\":\"1\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/S0927776525001705\",\"RegionNum\":2,\"RegionCategory\":\"医学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q1\",\"JCRName\":\"BIOPHYSICS\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Colloids and Surfaces B: Biointerfaces","FirstCategoryId":"1","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S0927776525001705","RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q1","JCRName":"BIOPHYSICS","Score":null,"Total":0}
Stabilizing effect of quercetin upon bovine serum albumin as a model protein
Quercetin (QCT), an emerging class of flavonoid known for antioxidant and anti-inflammatory activities, has been studied for its protein stabilizing effect. After demonstrating ethanol (EtOH) - induced structural changes in bovine serum albumin (BSA), the stabilizing effect of QCT was studied using fluorescence, circular dichroism (CD) and Fourier transform infrared (FTIR) spectroscopic techniques. Morphological changes were examined using atomic force microscopy (AFM). EtOH triggered blue shift in fluorescence spectra of BSA and its intensity increased at higher percentage of alcohol. A reversal in this trend was recorded in the presence of QCT. This was interpreted as anti-amyloidogenic effect emanating from the binding of QCT to hydrophobic pockets of BSA. The value of binding constant (1.25 x 106 M−1; 298 K) is suggestive of strong binding affinity of QCT for BSA. The mode of QCT-induced fluorescence quenching was found to be mixed in nature. CD spectra showed that the protein conformation was altered and traces of alpha helix disappeared in the presence of EtOH. Contrarily, disruptive effect of EtOH was not visible upon incorporating QCT. This was further verifiable form the thermal CD data, which showed an upshift in the denaturation temperature of BSA. The data of thioflavin T assay and AFM further substantiated the protective effect of QCT.
期刊介绍:
Colloids and Surfaces B: Biointerfaces is an international journal devoted to fundamental and applied research on colloid and interfacial phenomena in relation to systems of biological origin, having particular relevance to the medical, pharmaceutical, biotechnological, food and cosmetic fields.
Submissions that: (1) deal solely with biological phenomena and do not describe the physico-chemical or colloid-chemical background and/or mechanism of the phenomena, and (2) deal solely with colloid/interfacial phenomena and do not have appropriate biological content or relevance, are outside the scope of the journal and will not be considered for publication.
The journal publishes regular research papers, reviews, short communications and invited perspective articles, called BioInterface Perspectives. The BioInterface Perspective provide researchers the opportunity to review their own work, as well as provide insight into the work of others that inspired and influenced the author. Regular articles should have a maximum total length of 6,000 words. In addition, a (combined) maximum of 8 normal-sized figures and/or tables is allowed (so for instance 3 tables and 5 figures). For multiple-panel figures each set of two panels equates to one figure. Short communications should not exceed half of the above. It is required to give on the article cover page a short statistical summary of the article listing the total number of words and tables/figures.