A molecular dynamics study on the binding of gemcitabine to human serum albumin

Volume: 337, Pages: 116496 - 116496
Published: Sep 1, 2021
Abstract
• HSA Sudlow sites (Ⅰ and Ⅱ) have a great capacity to adsorb considerable amounts of drugs. • GEM loading on these sites induced slight conformational changes in the HSA structure. • It also reduces the accumulated surface energy on these Sudlow sites. • The results show, H bonding is the main force of the stability of the GEM-HSA complex. • All observations also prove that the GEM on the Sudlow site Ⅱ has a higher stability. Human Serum Albumin...
Paper Details
Title
A molecular dynamics study on the binding of gemcitabine to human serum albumin
Published Date
Sep 1, 2021
Volume
337
Pages
116496 - 116496
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