Adsorption of Random Coils and Helices at SOLID/LIQUID Interfaces: A Monte Carlo Study

Abstract

Polyamino acids are useful models for understanding the contribution of individual amino acids to the protein adsorption process. in this study, MC simulations were used to study a ten residues peptide in water and vacuum at charged surfaces. the peptides were folded into an α-helix and a random coil configuration. the procedure developed by Mungikar and Forciniti [A. Mungikar, D. Forciniti, Biomacromolecules, 5 (2004) 2147] was adopted to perform the MC simulations. for both helix and random coil conformations, in water as well as vacuum, the Lys-block rests near the surface whereas its Ala-block is relatively away from the surface. Electrostatic forces drive the adsorption of the peptide at the solid surface. in water, the helical peptide adsorbed in a side-on orientation whereas the random coil peptide had its Ala-block extended into the bulk. This apparent 'repulsion' for the surface is actually due to the effect of solvent and is not seen in vacuum. the adsorption process consists of rapid anchoring of a couple of Lys residues into the surface followed by a slow relaxation process caused by maximizing contacts between Lys residues and the surface.

Department(s)

Chemical and Biochemical Engineering

Keywords and Phrases

Adsorption; Monte Carlo; Peptide

Document Type

Article - Conference proceedings

Document Version

Citation

File Type

text

Language(s)

English

Rights

© 2024 Interamerican Congress of Chemical Engneering, All rights reserved.

Publication Date

01 Jan 2006

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