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	<title>ligand-receptor interaction &#8211; BIOENGINEER.ORG</title>
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		<title>Bisphenol Substitutes Bind Estrogen Receptor More Tightly Than Estradiol Itself, Simulation Study Finds</title>
		<link>https://bioengineer.org/bisphenol-substitutes-bind-estrogen-receptor-more-tightly-than-estradiol-itself-simulation-study-finds/</link>
		
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		<pubDate>Mon, 12 Oct 2026 07:47:56 +0000</pubDate>
				<category><![CDATA[Chemistry]]></category>
		<category><![CDATA[17β-estradiol]]></category>
		<category><![CDATA[allosteric signaling]]></category>
		<category><![CDATA[bisphenol A]]></category>
		<category><![CDATA[bisphenol PH]]></category>
		<category><![CDATA[endocrine disruptors]]></category>
		<category><![CDATA[estrogen receptor alpha]]></category>
		<category><![CDATA[helix-12]]></category>
		<category><![CDATA[ligand-receptor interaction]]></category>
		<category><![CDATA[MM/PBSA]]></category>
		<category><![CDATA[molecular docking]]></category>
		<category><![CDATA[Molecular dynamics simulation]]></category>
		<category><![CDATA[Toxicology]]></category>
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					<description><![CDATA[A computational study finds that bisphenol PH, a BPA substitute, binds estrogen receptor alpha more strongly than estradiol and disrupts the receptor's helix-12 signaling dynamics in distinct ligand-specific ways.]]></description>
		
		
		
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