title: Coarse-grained molecular dynamics of ligands binding into protein: The case of HIV-1 protease inhibitors.
abstract: Binding dynamics and pathways of ligands or inhibitors to target proteins are challenging both experimental and theoretical biologists. A dynamics understanding of inhibitors interacting with protein is essential for the design of novel potent drugs. In this work we applied a coarse-grained molecular dynamics method for simulating inhibitors entering the binding cavity of human immunodeficiency virus type 1 protease (PR). It shows that the coarse-grained dynamics, consistent with the experimental results, can capture the essential molecular dynamics of various inhibitors binding into PR. The primary driving force for the binding processes is the nonbond interaction between inhibitors and PR. The size and topology of inhibitors and the interacting strength between inhibitors and PR have great influence on the binding mode and processes. The interaction strength between the PR and various inhibitors is also analyzed by atomistic molecular mechanics and Poisson-Boltzmann solvation area method.
authors.affiliation: Department of Engineering Mechanics, School of Aerospace, Tsinghua University, Beijing 100084, China.
authors.forename: Dechang
authors.initials: D
authors.lastname: Li
authors.forename: Ming S
authors.initials: MS
authors.lastname: Liu
authors.forename: Baohua
authors.initials: B
authors.lastname: Ji
authors.forename: Kehchih
authors.initials: K
authors.lastname: Hwang
authors.forename: Yonggang
authors.initials: Y
authors.lastname: Huang
mesh_terms: D016333:HIV Protease / Q000737:chemistry* / Q000378:metabolism; D017320:HIV Protease Inhibitors / Q000737:chemistry* / Q000378:metabolism / Q000494:pharmacology; D015497:HIV-1; D007700:Kinetics; D008024:Ligands; D008958:Models, Molecular; D011485:Protein Binding; D011487:Protein Conformation; D013816:Thermodynamics
chemical_list: D017320:HIV Protease Inhibitors; D008024:Ligands; D016333:HIV Protease