Controlling noncovalent interactions between a lysine-rich α-helical peptide and self-assembled monolayers of alkanethiols on Au through functional group diversity

0Citations
Citations of this article
15Readers
Mendeley users who have this article in their library.
Get full text

Abstract

Reliably attaching a structured biomolecule to an inorganic substrate would enable the preparation of surfaces that incorporate both biological and inorganic functions and structures. To this end, we have previously developed a procedure using the copper(I)-catalyzed click reaction to tether synthetic α-helical peptides carrying two alkyne groups to well-ordered alkanethiol self-assembled monolayers (SAM) on a Au(111) surface, in which the SAM is composed of a mixture of methyl and azide termination. Proteins, however, are composed of many diverse functional groups, and this composition directly effects protein structure, interactions, and reactivity. Here, we explore the utility of mixed SAMs with alternative terminating functional groups to tune and direct the reactivity of the surface through noncovalent peptide-surface interactions. We study both polar surfaces (OH-terminated) and charged surfaces (COOH- and NH 3 -terminated, which are negatively and positively charged, respectively, under our reaction conditions). Surfaces were functionalized with a bipolar peptide composed of Lys and Leu residues that could express different interactions through either hydrophilic and/or charge (Lys) or hydrophobic (Leu) influences. X-ray photoelectron spectroscopy (XPS) and surface infrared spectroscopy were used to characterize surfaces at all stages of the peptide functionalization procedure. This strategy resulted in a high density of surface-bound α-helices without aggregation. Mixed SAMs that included a positively charged alkanethiol along with the azide-terminated thiol resulted in a more efficient reaction and better alignment of the peptide with the azide on the surface. Negatively charged surfaces increased physisorption of the peptide, which was then removed during sample rinsing. This work demonstrates that varying easily controlled chemical inputs during the functionalization steps allows the reaction conditions to be balanced for the chemical needs of a particular biomolecule or substrate.

Cite

CITATION STYLE

APA

Raigoza, A. F., Onyirioha, K., & Webb, L. J. (2017). Controlling noncovalent interactions between a lysine-rich α-helical peptide and self-assembled monolayers of alkanethiols on Au through functional group diversity. Applied Surface Science, 396, 1831–1839. https://doi.org/10.1016/j.apsusc.2016.11.177

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free