Computational View of β-Asarone–Human Serum Albumin Interaction
2021 ◽
Vol 12
(4)
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pp. 5296-5302
Keyword(s):
β-Asarone (BAS), a bioactive phytochemical from the medicinal herb, Acorus calamus Linn., has shown many pharmacological activities. Computational docking studies unveiled the interaction site of BAS on the human plasma carrier, albumin. The primary binding arrangement of BAS was placed at Sudlow's Site I of HSA, which is pinpointed in subdomain IIA of albumin. Hydrophobic and van der Waals forces together with hydrogen bonds appear to secure the BAS-albumin complex. The BAS at Site I was surrounded by more hydrophobic and polar residues than those seen at Site II, as evidenced by LigPlot+. Therefore, the interaction between BAS and albumin at Site I seems to be comparatively more stable owing to more vital interactions.
2013 ◽
Vol 2013
(26)
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pp. 4619-4627
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Keyword(s):
2018 ◽
Vol 43
(6)
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pp. 369-375
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Keyword(s):
2021 ◽
Vol 246
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pp. 119000
Keyword(s):
2019 ◽
Vol 222
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pp. 117158
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Keyword(s):
1986 ◽
Vol 136
(3)
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pp. 983-988
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Keyword(s):
2004 ◽
Vol 69A
(4)
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pp. 748-756
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Keyword(s):
Protein binding of atenolol and propranolol to human serum albumin and in human plasma [proceedings]
1978 ◽
Vol 6
(5)
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pp. 446P-447P
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1944 ◽
Vol 23
(4)
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pp. 445-453
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Keyword(s):
1944 ◽
Vol 23
(4)
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pp. 491-505
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Keyword(s):