Dataset Information

Adsorption of cationic peptides to solid surfaces of glass and plastic.

ABSTRACT: Cationic membrane-active peptides have been studied for years in the hope of developing them into novel types of therapeutics. In this article, we investigate an effect that might have significant experimental implications for investigators who wish to study these peptides, namely, that the peptides adsorb to solid surfaces of glass and plastic. Specifically, we use analytical HPLC to systematically quantify the adsorption of the three cationic membrane-active peptides mastoparan X, melittin, and magainin 2 to the walls of commonly used glass and plastic sample containers. Our results show that, at typical experimental peptide concentrations, 90% or more of the peptides might be lost from solution due to rapid adsorption to the walls of the sample containers. Thus, our results emphasize that investigators should always keep these adsorption effects in mind when designing and interpreting experiments on cationic membrane-active peptides. We conclude the article by discussing different strategies for reducing the experimental impact of these adsorption effects.

SUBMITTER: Kristensen K

PROVIDER: S-EPMC4416745 | biostudies-literature | 2015

REPOSITORIES: biostudies-literature

ACCESS DATA

Publications

Adsorption of cationic peptides to solid surfaces of glass and plastic.

Kristensen Kasper K Henriksen Jonas R JR Andresen Thomas L TL

PloS one 20150501 5

Cationic membrane-active peptides have been studied for years in the hope of developing them into novel types of therapeutics. In this article, we investigate an effect that might have significant experimental implications for investigators who wish to study these peptides, namely, that the peptides adsorb to solid surfaces of glass and plastic. Specifically, we use analytical HPLC to systematically quantify the adsorption of the three cationic membrane-active peptides mastoparan X, melittin, an ...[more]

PMID: 25932639

Similar Datasets

Project description:The adsorption of amyloidogenic peptides, amyloid beta 1-40 (A?1-40), alpha-synuclein (?-syn), and beta 2 microglobulin (?2m), was attempted over the surface of nano-gold colloidal particles, ranging from d = 10 to 100 nm in diameter (d). The spectroscopic inspection between pH 2 and pH 12 successfully extracted the critical pH point (pHo) at which the color change of the amyloidogenic peptide-coated nano-gold colloids occurred due to aggregation of the nano-gold colloids. The change in surface property caused by the degree of peptide coverage was hypothesized to reflect the ?pHo, which is the difference in pHo between bare gold colloids and peptide coated gold colloids. The coverage ratio (?) for all amyloidogenic peptides over gold colloid of different sizes was extracted by assuming ? = 0 at ?pHo = 0. Remarkably, ? was found to have a nano-gold colloidal size dependence, however, this nano-size dependence was not simply correlated with d. The geometric analysis and simulation of reproducing ? was conducted by assuming a prolate shape of all amyloidogenic peptides. The simulation concluded that a spiking-out orientation of a prolate was required in order to reproduce the extracted ?. The involvement of a secondary layer was suggested; this secondary layer was considered to be due to the networking of the peptides. An extracted average distance of networking between adjacent gold colloids supports the binding of peptides as if they are "entangled" and enclosed in an interfacial distance that was found to be approximately 2 nm. The complex nano-size dependence of ? was explained by available spacing between adjacent prolates. When the secondary layer was formed, A?1-40 and ?-syn possessed a higher affinity to a partially negative nano-gold colloidal surface. However, ?2m peptides tend to interact with each other. This difference was explained by the difference in partial charge distribution over a monomer. Both A?1-40 and ?-syn are considered to have a partial charge (especially ?+) distribution centering around the prolate axis. The ?2m, however, possesses a distorted charge distribution. For a lower ? (i.e., ? <0.5), a prolate was assumed to conduct a gyration motion, maintaining the spiking-out orientation to fill in the unoccupied space with a tilting angle ranging between 5° and 58° depending on the nano-scale and peptide coated to the gold colloid.

Dataset Information

Adsorption of cationic peptides to solid surfaces of glass and plastic.

Publications

Adsorption of cationic peptides to solid surfaces of glass and plastic.

Similar Datasets

OmicsDI is part of the ELIXIR infrastructure

Tweets