ArticleBiointerphases2010
Kinetics of leucine-lysine peptide adsorption and desorption at -CH3 and -COOH terminated alkylthiolate monolayers.
Article in Biointerphases, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
3 citing papers in PubMed, 17 citations in OpenAlex.
- The Adsorption of P2X2 Receptors Interacting with IgG Antibodies Revealed by Combined AFM Imaging and Mechanical Simulation.International journal of molecular sciences · 2023Article
- Interplay between adsorbed peptide structure, trapped water, and surface hydrophobicity.Biointerphases · 2017Article
- Effect of thermal stability on protein adsorption to silica using homologous aldo-keto reductases.Protein science : a publication of the Protein Society · 2012Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The kinetics of adsorption and desorption of two highly asymmetrical model peptides were studied at methyl- and carboxylic acid-terminated alkylthiolate self-assembled monolayer (SAM) surfaces on gold. The model peptides were leucine-lysine (LK), α-helical (LKα14), and β-strand (LKβ15) peptides that have a well-defined secondary structure with the leucines localized on one side and the lysines on the other side. These secondary structures were previously shown to be maintained after adsorption and to control LK peptide orientation on these surfaces. The kinetics of peptide adsorption were analyzed by surface plasmon resonance as a function of peptide solution concentrations at pH 7.4. Peptide desorption was measured by rinsing with a buffer at various times along the adsorption curve. Both peptides had a saturation coverage of approximately 1 ML (monolayer) on the carboxyl SAM. Both peptides exhibited mostly irreversible binding on both surfaces, but the LKα14 peptide showed some limited reversible binding. Reversibly bound peptides could be in the second adlayer interacting only with peptides in the first layer or peptides interacting with a partially covered adsorption site and therefore not able to fully bind to the SAM surface. The near complete lack of reversible binding for LKβ15 is possibly due to strong peptide-peptide hydrogen bonding in β-sheet structures within the adsorbed layer. For a given dose of either peptide, much less peptide adsorbed on the methyl SAMs. The adsorption rate of irreversibly bound LKα14 on carboxylic acid SAMs was first-order with respect to solution concentration. Both peptides showed nucleation-like adsorption kinetics on the carboxylic acid SAM, indicating that peptide-peptide bonding is needed to stabilize the adsorbed layer. Adsorption on the methyl SAM was much lower in quantity for both peptides and seemed to require prior aggregation of the proteins in solution, at least for LKβ15.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.