Investigating the Effects of Aromatic Amino Acids on Amphipathic Peptide Self-Assembly and Emergent Hydrogel Viscoelasticity

Rajbhandary, Annada; Nilsson, Bradley L.

doi:10.17952/24aps.2015.228

Cited by 2 publications

(1 citation statement)

References 8 publications

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“…This thixotropic property allows the supramolecular gel particles to gradually dissolve and release the drug through oral administration, which can achieve the goal of sustained release drugs in a period of time. These gel particles can also stabilize water-soluble compounds, especially for reducing the enzymatic hydrolysis of peptide compounds like the insulin, and are often used as the study of controlled release systems for water-soluble compounds [38] .…”

Section: Nanogelmentioning

confidence: 99%

Developments in encapsulation of insulin: Is oral delivery now possible?

Pratap-Singh

Guo

Xie

et al. 2019

J Pharm Biopharm Res

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This review presents the possibilities of oral delivery of insulin. Insulin, being readily destroyed/transformed by the proteolytic enzymes and first-pass effects in the digestive system, has mainly been administered through injection, such as intravenous injection and transdermal injection. With developments in the material sciences, appropriate encapsulation methodologies have been developed that could be employed to protect insulin from the digestive effects of the human GI system, and thereby have opened a gateway of research exploring the oral route of insulin delivery. One approach is to incorporate insulin into an emulsion with an appropriate oil-phase, which protects the insulin from degradation. Coating with natural or synthetic polymeric materials, or with lipids, followed by size-reduction to 100-1000 nm is applied as another common approaches of insulin encapsulation. Other approaches like liposomes, nanogels, etc. are also being explored. This review gives a summary of methods of preparation as well as in vitro and in vivo bioavailability of insulin through these methods. It is observed that the oral bioavailability of insulin intake has increased from about 0.1% to about 20% for encapsulated insulin.

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Section: Nanogelmentioning

confidence: 99%

Developments in encapsulation of insulin: Is oral delivery now possible?

Pratap-Singh

Guo

Xie

et al. 2019

J Pharm Biopharm Res

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Peptide Sequence Variations Govern Hydrogel Stiffness: Insights from a Multi‐Scale Structural Analysis of H‐FQFQFK‐NH₂Peptide Derivatives

De Maeseneer,

Cauwenbergh,

Gardiner

et al. 2024

Macromolecular Bioscience

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Throughout the past decades, amphipathic peptide‐based hydrogels have proven to be promising materials for biomedical applications. Amphipathic peptides are known to adopt β‐sheet configurations that self‐assemble into fibers that then interact to form a hydrogel network. A fundamental understanding of how the peptide sequence alters the structural properties of the hydrogels would allow for a more rational design of novel peptides for a variety of biomedical applications in the future. Therefore, the current work investigates how changing the type of amino acid, the amphipathic pattern, and the peptide length affects the secondary structure, fiber characteristics and stiffness of peptide‐based hydrogels. Hereto, seven amphipathic peptides of different sequence and length, four of which have not been previously reported, based on and including the hexapeptide H‐Phe‐Gln‐Phe‐Gln‐Phe‐Lys‐NH2, were synthesized and thoroughly characterized by CD, FTIR, WAXS, SAXS, TEM and ThT fibrillization assays. The results show that a high amount of regularly spaced β‐sheets, a high amount of fibers and fiber bundling contribute to the stiffness of the hydrogel. Furthermore, a study of the time‐dependent fibril formation process reveals complex transient dynamics. The peptide strands structure through an intermediate helical state prior to β‐sheet formation, which is found to be concentration‐ and time‐dependent.This article is protected by copyright. All rights reserved

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Investigating the Effects of Aromatic Amino Acids on Amphipathic Peptide Self-Assembly and Emergent Hydrogel Viscoelasticity

Cited by 2 publications

References 8 publications

Developments in encapsulation of insulin: Is oral delivery now possible?

Developments in encapsulation of insulin: Is oral delivery now possible?

Peptide Sequence Variations Govern Hydrogel Stiffness: Insights from a Multi‐Scale Structural Analysis of H‐FQFQFK‐NH₂Peptide Derivatives

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Investigating the Effects of Aromatic Amino Acids on Amphipathic Peptide Self-Assembly and Emergent Hydrogel Viscoelasticity

Cited by 2 publications

References 8 publications

Developments in encapsulation of insulin: Is oral delivery now possible?

Developments in encapsulation of insulin: Is oral delivery now possible?

Peptide Sequence Variations Govern Hydrogel Stiffness: Insights from a Multi‐Scale Structural Analysis of H‐FQFQFK‐NH2Peptide Derivatives

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Peptide Sequence Variations Govern Hydrogel Stiffness: Insights from a Multi‐Scale Structural Analysis of H‐FQFQFK‐NH₂Peptide Derivatives