In silico identification of the anticataract target of βB2-crystallin from Phaseolus vulgaris: a new insight into cataract treatment
IntroductionSevere protein clumping in the lens can block light and lead to vision issues in cataract patients. Recent studies have linked β-crystallins, which are key proteins in the lens, to the development of cataracts. Specifically, the S175G/H181Q mutation in the βB2-crystallin gene plays a maj...
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Frontiers Media S.A.
2025-01-01
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| Online Access: | https://www.frontiersin.org/articles/10.3389/fchem.2024.1421534/full |
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| author | Sunday Amos Onikanni Sunday Amos Onikanni Adewale Oluwaseun Fadaka Tran Nhat Phong Dao Tran Nhat Phong Dao Valens Munyembaraga Valens Munyembaraga Vincent Nyau Nicole Remaliah Samantha Sibuyi Morenike Grace Ajayi Nguyen Thi Ai Nhung Emmanuel Ejiofor Basiru Olaitan Ajiboye Basiru Olaitan Ajiboye Minh Hoang Le Hen-Hong Chang Hen-Hong Chang Hen-Hong Chang |
| author_facet | Sunday Amos Onikanni Sunday Amos Onikanni Adewale Oluwaseun Fadaka Tran Nhat Phong Dao Tran Nhat Phong Dao Valens Munyembaraga Valens Munyembaraga Vincent Nyau Nicole Remaliah Samantha Sibuyi Morenike Grace Ajayi Nguyen Thi Ai Nhung Emmanuel Ejiofor Basiru Olaitan Ajiboye Basiru Olaitan Ajiboye Minh Hoang Le Hen-Hong Chang Hen-Hong Chang Hen-Hong Chang |
| author_sort | Sunday Amos Onikanni |
| collection | DOAJ |
| description | IntroductionSevere protein clumping in the lens can block light and lead to vision issues in cataract patients. Recent studies have linked β-crystallins, which are key proteins in the lens, to the development of cataracts. Specifically, the S175G/H181Q mutation in the βB2-crystallin gene plays a major role in cataract formation.MethodsTo understand how this mutation can be activated, we utilized computational methods to predict activators from Phaseolus vulgaris. The Schrödinger platform was employed to screen bioactive compounds and simulate molecular interactions in order to analyze binding and structural changes.ResultsOur results indicated that these phytochemicals are stable near S175G/H181Q.DiscussionThese findings suggest novel approaches that could potentially be developed into effective anticataract medications through further refinement and additional testing, ultimately resulting in the creation of more potent agents for cataract treatment. |
| format | Article |
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| institution | Kabale University |
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| language | English |
| publishDate | 2025-01-01 |
| publisher | Frontiers Media S.A. |
| record_format | Article |
| series | Frontiers in Chemistry |
| spelling | doaj-art-36c80eb4978a4c32a8822d3619f969e62025-01-17T06:51:18ZengFrontiers Media S.A.Frontiers in Chemistry2296-26462025-01-011210.3389/fchem.2024.14215341421534In silico identification of the anticataract target of βB2-crystallin from Phaseolus vulgaris: a new insight into cataract treatmentSunday Amos Onikanni0Sunday Amos Onikanni1Adewale Oluwaseun Fadaka2Tran Nhat Phong Dao3Tran Nhat Phong Dao4Valens Munyembaraga5Valens Munyembaraga6Vincent Nyau7Nicole Remaliah Samantha Sibuyi8Morenike Grace Ajayi9Nguyen Thi Ai Nhung10Emmanuel Ejiofor11Basiru Olaitan Ajiboye12Basiru Olaitan Ajiboye13Minh Hoang Le14Hen-Hong Chang15Hen-Hong Chang16Hen-Hong Chang17College of Medicine, Graduate Institute of Biomedical Sciences, China Medical University, Taichung, TaiwanDepartment of Chemical Sciences, Biochemistry Unit, Afe-Babalola University, Ado-Ekiti, NigeriaDepartment of Biotechnology, University of the Western Cape, Bellville, South AfricaGraduate Institute of Integrated Medicine, College of Chinese Medicine, China Medical University, Taichung, TaiwanFaculty of Traditional Medicine, Can Tho University of Medicine and Pharmacy, Can Tho, VietnamInstitute of Translational Medicine and New Drug Development, College of Medicine, China Medical University, Taichung, TaiwanUniversity Teaching Hospital of Butare, Huye, RwandaDepartment of Food Science and Nutrition, School of Agricultural Sciences, University of Zambia, Lusaka, ZambiaDepartment of Science and Innovation/Mintek Nanotechnology Innovation Centre, Biolabels Node, University of the Western Cape, Bellville, South Africa0Department of Chemical Sciences, Bamidele Olumilua University of Education, Science and Technology, Ikere, Nigeria1Department of Chemistry, University of Sciences, Hue University, Hue, Vietnam2Department of Chemical Sciences, Faculty of Science, Clifford University, Owerrinta, Nigeria3Phytomedicine and Molecular Toxicology Research Laboratory, Department of Biochemistry, Federal University Oye Ekiti, Oye Ekiti, Nigeria4Institute of Drug Research and Development, SE Bogoro Center, Afe Babalola University, PMB5454, Ado-Ekiti, NigeriaFaculty of Traditional Medicine, Can Tho University of Medicine and Pharmacy, Can Tho, VietnamGraduate Institute of Integrated Medicine, College of Chinese Medicine, China Medical University, Taichung, Taiwan5Chinese Medicine Research Centre, China Medical University, Taichung, Taiwan6Department of Chinese Medicine, China Medical University Hospital, Taichung, TaiwanIntroductionSevere protein clumping in the lens can block light and lead to vision issues in cataract patients. Recent studies have linked β-crystallins, which are key proteins in the lens, to the development of cataracts. Specifically, the S175G/H181Q mutation in the βB2-crystallin gene plays a major role in cataract formation.MethodsTo understand how this mutation can be activated, we utilized computational methods to predict activators from Phaseolus vulgaris. The Schrödinger platform was employed to screen bioactive compounds and simulate molecular interactions in order to analyze binding and structural changes.ResultsOur results indicated that these phytochemicals are stable near S175G/H181Q.DiscussionThese findings suggest novel approaches that could potentially be developed into effective anticataract medications through further refinement and additional testing, ultimately resulting in the creation of more potent agents for cataract treatment.https://www.frontiersin.org/articles/10.3389/fchem.2024.1421534/fullβB2-crystallinPhaseolus vulgariscataractSchrödingerconformation |
| spellingShingle | Sunday Amos Onikanni Sunday Amos Onikanni Adewale Oluwaseun Fadaka Tran Nhat Phong Dao Tran Nhat Phong Dao Valens Munyembaraga Valens Munyembaraga Vincent Nyau Nicole Remaliah Samantha Sibuyi Morenike Grace Ajayi Nguyen Thi Ai Nhung Emmanuel Ejiofor Basiru Olaitan Ajiboye Basiru Olaitan Ajiboye Minh Hoang Le Hen-Hong Chang Hen-Hong Chang Hen-Hong Chang In silico identification of the anticataract target of βB2-crystallin from Phaseolus vulgaris: a new insight into cataract treatment Frontiers in Chemistry βB2-crystallin Phaseolus vulgaris cataract Schrödinger conformation |
| title | In silico identification of the anticataract target of βB2-crystallin from Phaseolus vulgaris: a new insight into cataract treatment |
| title_full | In silico identification of the anticataract target of βB2-crystallin from Phaseolus vulgaris: a new insight into cataract treatment |
| title_fullStr | In silico identification of the anticataract target of βB2-crystallin from Phaseolus vulgaris: a new insight into cataract treatment |
| title_full_unstemmed | In silico identification of the anticataract target of βB2-crystallin from Phaseolus vulgaris: a new insight into cataract treatment |
| title_short | In silico identification of the anticataract target of βB2-crystallin from Phaseolus vulgaris: a new insight into cataract treatment |
| title_sort | in silico identification of the anticataract target of βb2 crystallin from phaseolus vulgaris a new insight into cataract treatment |
| topic | βB2-crystallin Phaseolus vulgaris cataract Schrödinger conformation |
| url | https://www.frontiersin.org/articles/10.3389/fchem.2024.1421534/full |
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