{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,20]],"date-time":"2026-08-20T14:51:10Z","timestamp":1787237470000,"version":"build-2736575974"},"reference-count":52,"publisher":"Bentham Science Publishers Ltd.","issue":"2","content-domain":{"domain":["eurekaselect.com"],"crossmark-restriction":true},"short-container-title":["CPB"],"published-print":{"date-parts":[[2021,2]]},"abstract":"<jats:sec>\n                    <jats:title>Background:<\/jats:title>\n                    <jats:p>Several human diseases like Parkinson\u2019s, Alzheimer\u2019s disease, and systemic\namyloidosis are associated with the misfolding and aggregation of protein molecules.<\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Objective:<\/jats:title>\n                    <jats:p>The present study demonstrated the comparison of 4-methyl coumarin and 4-methylthiocoumarin\nderivative for their anti-amyloidogenic and disaggregation activities. The hen egg-white lysozyme\nis used as a model system to study protein aggregation and disaggregation under in vitro conditions.<\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Methods:<\/jats:title>\n                    <jats:p>Techniques used in the study were Thioflavin T fluorescence assay, intrinsic fluorescence\nassay, circular dichroism, transmission electron microscopy, and molecular dynamics.<\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Results:<\/jats:title>\n                    <jats:p>Fifteen compounds were screened for their anti-amyloidogenic and disaggregation potential.\nSix compounds significantly inhibited the fibril formation, whereas ten compounds showed disaggregation\nproperty of pre-formed fibrils. Under in vitro conditions, the compound C3 and C7 showed significant\ninhibition of fibril formation in a concentration-dependent manner as compared to control. C3\nand C7 demonstrated 93% and 76% inhibition of fibril formation, respectively. Furthermore, C3 and\nC7 exhibited 83% and 76% disaggregation activity, respectively, of pre-formed HEWL fibrils at their\nhighest concentration. These anti-amyloidogenic and disaggregation potential of C3 and C7 were validated\nby intrinsic fluorescence, CD, molecular dynamics, and TEM study.<\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Discussion:<\/jats:title>\n                    <jats:p>4-methylthiocoumarins derivatives have shown better anti-amyloidogenic activity as compared\nto 4-methylcoumarin derivatives for both amyloid formation as well as disaggregation of preformed\namyloid fibrils. Structurally, the derivatives of 4-methylthiocoumarins (C3 and C7) contain\nthio group on 2nd position that might be responsible for anti-amyloidogenic activity as compared to 4-\nmethylcoumarin derivatives (C2 and C4).<\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Conclusion:<\/jats:title>\n                    <jats:p>C3 and C7 are novel 4-methylthiocoumarin derivatives that can be used as a lead for\nalleviation and symptoms associated with protein aggregation disorders.<\/jats:p>\n                  <\/jats:sec>","DOI":"10.2174\/1389201021666200915112849","type":"journal-article","created":{"date-parts":[[2020,9,16]],"date-time":"2020-09-16T00:06:39Z","timestamp":1600214799000},"page":"232-244","update-policy":"https:\/\/doi.org\/10.2174\/bsp_crossmark_policy","source":"Crossref","is-referenced-by-count":3,"title":["Inhibition of Amyloid Fibrillation of HEWL by 4-Methylcoumarin and 4-Methylthiocoumarin Derivatives"],"prefix":"10.2174","volume":"22","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-7940-2007","authenticated-orcid":true,"given":"Shivani","family":"Kumar","sequence":"first","affiliation":[{"name":"University School of Biotechnology Guru Gobind Singh Indraprastha University Dwarka, Sector 16C, New Delhi- 110078,India"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-8239-7253","authenticated-orcid":true,"given":"Manoj","family":"Kumar","sequence":"additional","affiliation":[{"name":"Department of Biophysics, All India Institute of Medical Sciences, New Delhi-110029,India"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-4558-8197","authenticated-orcid":true,"given":"Yogesh K.","family":"Tyagi","sequence":"additional","affiliation":[{"name":"University School of Basic and Applied Sciences Guru Gobind Singh Indraprastha University Dwarka, Sector 16C, New Delhi- 110078,India"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-2637-3927","authenticated-orcid":true,"given":"Suresh","family":"Kumar","sequence":"additional","affiliation":[{"name":"University School of Biotechnology Guru Gobind Singh Indraprastha University Dwarka, Sector 16C, New Delhi- 110078,India"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"965","reference":[{"key":"ref=1","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pone.0142095","volume":"10","author":"Chaari A.","year":"2015","unstructured":"Chaari A.; Fahy C.; Chevillot-Biraud A.; Rholam M.; Insights into kinetics of agitation-induced aggregation of hen lysozyme under heat and acidic conditions from various spectroscopic methods. 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