Probing Amino Acid Interaction with a Polystyrene Nanoparticle Surface Using Saturation-Transfer Difference (STD)-NMR

Zhang, Yunzhi; Casabianca, Leah B.

doi:10.1021/acs.jpclett.8b02785

Cited by 32 publications

(29 citation statements)

References 42 publications

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“…Various components contained in the intestinal contents may interact with the surface molecules of NG(S). Such interaction of the medium component with NPs was reported by Zhang et al [34]. The modification of NG(S) by the components of the intestinal contents might influence the release patterns.…”

Section: Drug Distribution In the Gastrointestinal Tract After The Insupporting

confidence: 61%

“…Furthermore, according to the study by Yano et al [14], PD was quickly absorbed into the systemic circulation after oral dosing with a suspension of PD alone at 10 mg/kg. This good absorption of free PD is associated with side effects [14,34]. Therefore, the plasma PD levels detected were considered to be an indicator of the severity of side effects.…”

Section: Plasma Concentration Of Pd After the Intragastric Administramentioning

confidence: 99%

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Nanogels of a Succinylated Glycol Chitosan-Succinyl Prednisolone Conjugate: Release Behavior, Gastrointestinal Distribution, and Systemic Absorption

Zhou

Ikeuchi-Takahashi

Hattori

et al. 2020

IJMS

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Recently, the potential of nanoparticles (NPs) in ulcerative colitis (UC) therapy has been increasingly demonstrated. Namely, anionic NPs have been found to be accumulated efficiently to the UC damaged area due to epithelial enhanced permeability and retention (eEPR) effect. Previously, a novel anionic nanogel system (NG(S)) was prepared, and evaluated for the efficacy and toxicity. In the present study, release behaviors and biodistribution were investigated in detail to elucidate the functional mechanisms. Rats with 2,4,6-trinitrobenzene sulfonic acid (TNBS)-induced ulcerative colitis (UC) were used as biomodels. In vitro release was examined with or without the contents of the cecum or distal colon. Gastrointestinal distribution and plasma concentrations were investigated after the intragastric administration of 10 mg prednisolone (PD) eq./kg. At pH 1.2 and 6.8, release behaviors were slow, but controlled. Overall release was not markedly different irrespective of coexistence of intestinal contents. In in vivo studies, a large amount of PD was distributed in the lower parts of the gastrointestinal tract 6 and 12 h after administration with NG(S). PD accumulated well in the colonic parts, and prolonged release was noted. The systemic absorption of PD with NG(S) was hardly found. NG(S) concentrated the drug in the colon and showed controlled release. These behaviors were considered to lead to the previously reported good results, promotion of effectiveness and suppression of toxic side effects.

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Section: Drug Distribution In the Gastrointestinal Tract After The Insupporting

confidence: 61%

Section: Plasma Concentration Of Pd After the Intragastric Administramentioning

confidence: 99%

Nanogels of a Succinylated Glycol Chitosan-Succinyl Prednisolone Conjugate: Release Behavior, Gastrointestinal Distribution, and Systemic Absorption

Zhou

Ikeuchi-Takahashi

Hattori

et al. 2020

IJMS

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“…In the current work, we obtain more insight into the three modes of binding between amino acids and polystyrene nanoparticles that were proposed in our previous work 31 . By examining binding between charged amino acids and zwitterionic polystyrene beads at different pH values and salt concentrations, we find that electrostatic effects are important to binding.…”

Section: Discussionmentioning

confidence: 67%

“…In previous work 31 , we examined the binding between amino acids and polystyrene nanoparticles. We found significant STD effects for amino acids that have aromatic, positively-charged, or long aliphatic side chains, and attributed the binding between these amino acids and the polystyrene nanoparticles to pi-pi interactions, electrostatic interactions, and hydrophobic effects, respectively.…”

mentioning

confidence: 99%

Probing driving forces for binding between nanoparticles and amino acids by saturation-transfer difference NMR

Casabianca

2020

Sci Rep

Self Cite

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As nanotechnology becomes increasingly used in biomedicine, it is important to have techniques by which to examine the structure and dynamics of biologically-relevant molecules on the surface of engineered nanoparticles. Previous work has shown that Saturation-Transfer Difference (STD)-NMR can be used to explore the interaction between small molecules, including amino acids, and the surface of polystyrene nanoparticles. Here we use STD-NMR to further explore the different driving forces that are responsible for these interactions. Electrostatic effects are probed by using zwitterionic polystyrene beads and performing STD-NMR experiments at high, low, and neutral pH, as well as by varying the salt concentration and observing the effect on the STD buildup curve. The influence of dispersion interactions on ligand-nanoparticle binding is also explored, by establishing a structureactivity relationship for binding using a series of unnatural amino acids with different lengths of hydrophobic side chains. these results will be useful for predicting which residues in a peptide are responsible for binding and for understanding the driving forces for binding between peptides and nanoparticles in future studies.

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“…While this would suggest a hard corona and slow exchange behavior, a recent study by Yang et al . used saturation‐transfer difference (STD) NMR to investigate the association between amino acids and the polystyrene surface . STD NMR is similar to DEST in that off‐resonance saturation is used to monitor the strength of binding in an invisible, NP‐bound state.…”

Section: Results From Different Nanoparticle Systemsmentioning

confidence: 99%

Protein Interactions with Nanoparticle Surfaces: Highlighting Solution NMR Techniques

Perera

Hill

Fitzkee

2019

Israel Journal of Chemistry

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In the last decade, nanoparticles (NPs) have become a key tool in medicine and biotechnology as drug delivery systems, biosensors and diagnostic devices. The composition and surface chemistry of NPs vary based on the materials used: typically organic polymers, inorganic materials, or lipids. Nanoparticle classes can be further divided into sub-categories depending on the surface modification and functionalization. These surface properties matter when NPs are introduced into a physiological environment, as they will influence how nucleic acids, lipids, and proteins will interact with the NP surface. While small-molecule interactions are easily probed using NMR spectroscopy, studying protein-NP interactions using NMR introduces several challenges. For example, globular proteins may have a perturbed conforma-tion when attached to a foreign surface, and the size of NPprotein conjugates can lead to excessive line broadening. Many of these challenges have been addressed, and NMR spectroscopy is becoming a mature technique for in situ analysis of NP binding behavior. It is therefore not surprising that NMR has been applied to NP systems and has been used to study biomolecules on NP surfaces. Important considerations include corona composition, protein behavior, and ligand architecture. These features are difficult to resolve using classical surface and material characterization strategies, and NMR provides a complementary avenue of characterization. In this review, we examine how solution NMR can be combined with other analytical techniques to investigate protein behavior on NP surfaces.

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Probing Amino Acid Interaction with a Polystyrene Nanoparticle Surface Using Saturation-Transfer Difference (STD)-NMR

Cited by 32 publications

References 42 publications

Nanogels of a Succinylated Glycol Chitosan-Succinyl Prednisolone Conjugate: Release Behavior, Gastrointestinal Distribution, and Systemic Absorption

Nanogels of a Succinylated Glycol Chitosan-Succinyl Prednisolone Conjugate: Release Behavior, Gastrointestinal Distribution, and Systemic Absorption

Probing driving forces for binding between nanoparticles and amino acids by saturation-transfer difference NMR

Protein Interactions with Nanoparticle Surfaces: Highlighting Solution NMR Techniques

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