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Interaction of an ionic complementary peptide with a hydrophobic graphite surface
Author(s) -
Sheng Yuebiao,
Wang Wei,
Chen P.
Publication year - 2010
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1002/pro.444
Subject(s) - adsorption , peptide , hydrophobic effect , chemistry , ionic bonding , protonation , protein adsorption , electrostatics , molecular dynamics , monolayer , pyrolytic carbon , chemical engineering , organic chemistry , chemical physics , combinatorial chemistry , computational chemistry , ion , biochemistry , pyrolysis , engineering
Protein adsorption on a surface plays an important role in biomaterial science and medicine. It is strongly related to the interaction between the protein residues and the surface. Here we report all‐atom molecular dynamics simulations of the adsorption of an ionic complementary peptide, EAK16‐II, to the hydrophobic highly ordered pyrolytic graphite surface. We find that, the hydrophobic interaction is the main force to govern the adsorption, and the peptide interchain electrostatic interaction affects the adsorption rate. Under neutral pH condition, the interchain electrostatic attraction facilitates the adsorption, whereas under acidic and basic conditions, because of the protonation and deprotonation of glutamic acid and lysine residues, respectively, the resulting electrostatic repulsion slows down the adsorption. We also found that under basic condition, during the adsorption peptide Chain II will be up against a choice to adsorb to the surface through the hydrophobic interaction or to form a temporary hydrophobic core with the deposited peptide Chain I. These results provide a basis for understanding some of the fundamental interactions governing peptide adsorption on the surface, which can shed new light on novel applications, such as the design of implant devices and drug delivery materials.