Self‐assembling Peptides with Internal Ionizable Unnatural Amino Acids: A General Approach to pH‐responsive Peptide Materials

Asokan-Sheeja, Haritha; Yang, Su; Adones, Ashley A.; Chen, Weike; Fulton, Brandon; Chintapula, Uday; Nguyen, Kytai T.; Lovely, Carl J.; Brautigam, Chad A.; Nam, Kwangho; Dong, He

doi:10.1002/asia.202200724

Cited by 3 publications

(1 citation statement)

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“…To simplify synthesis and enable scalability, we designed the sequence K(QW)(QL) 3 K, where X = 1, Y = 4, and Z = 1 with one of the L residues replaced by W (tryptophan) for ultraviolet–visible (UV–vis)-based concentration measurements. As demonstrated in our previous research, − the alternating hydrophilic–hydrophobic pattern of (QW)(QL)3 promotes the formation of sandwich-like nanofiber structures with leucines and tryptophan embedded within the hydrophobic core of the assembly. The specific values chosen for X , Y , and Z were intended to enhance the solubility of the peptide assemblies while preserving the formation of secondary structures, as established in prior work. ,− …”

Section: Resultssupporting

confidence: 53%

In Situ Synthesis and Self-Assembly of Peptide–PEG Conjugates: A Facile Method for the Construction of Fibrous Hydrogels

Asokan-Sheeja,

Awad,

et al. 2024

Biomacromolecules

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Peptide-based hydrogels have gained considerable attention as a compelling platform for various biomedical applications in recent years. Their attractiveness stems from their ability to seamlessly integrate diverse properties, such as biocompatibility, biodegradability, easily adjustable hydrophilicity/hydrophobicity, and other functionalities. However, a significant drawback is that most of the functional self-assembling peptides cannot form robust hydrogels suitable for biological applications. In this study, we present the synthesis of novel peptide−PEG conjugates and explore their comprehensive hydrogel properties. The hydrogel comprises double networks, with the first network formed through the self-assembly of peptides to create a β-sheet secondary structure. The second network is established through covalent bond formation via N-hydroxysuccinimide chemistry between peptides and a 4-arm PEG to form a covalently linked network. Importantly, our findings reveal that this hydrogel formation method can be applied to other peptides containing lysine-rich sequences. Upon encapsulation of the hydrogel with antimicrobial peptides, the hydrogel retained high bacterial killing efficiency while showing minimum cytotoxicity toward mammalian cells. We hope that this method opens new avenues for the development of a novel class of peptide−polymer hydrogel materials with enhanced performance in biomedical contexts, particularly in reducing the potential for infection in applications of tissue regeneration and drug delivery.

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Section: Resultssupporting

confidence: 53%

In Situ Synthesis and Self-Assembly of Peptide–PEG Conjugates: A Facile Method for the Construction of Fibrous Hydrogels

Asokan-Sheeja,

Awad,

et al. 2024

Biomacromolecules

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Building structured, functional materials inspired by nature: Using peptides, peptoids, and polymerizations

Montz,

Emrick

2023

Journal of Polymer Science

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The assembly of peptide and peptide‐inspired building blocks into functional, well‐defined, multi‐length scale materials represents an exciting, rapidly expanding research field that bridges the principles of polymer science and engineering with a tremendous breadth of biomolecular interactions. The advantageous features of peptides, including their biocompatibility, functional diversity, and high purity, are complemented by the breadth of potential applications that may arise from their resultant structures and assemblies. Applications in biology (tissue scaffolding and drug conjugation), electronics (electron and/or ion‐conduction), and membranes (ion capture and ultrafiltration) represent a few of many examples where such biologically rich materials hold potential for enabling new routes to enhanced materials performance. Achieving successful solution and interfacial assembly techniques for peptides and other peptidomimetic materials requires obtaining a deep understanding of their design principles and limitations, as well as their amenability to structure formation when subjected to a variety of environmental conditions, such as pH, solvent, and temperature, to which such assembly methods may be exquisitely sensitive. This review especially focuses on mechanisms and the product of oligo‐ and polypeptide assembly, often resulting in the formation of extended, wire‐like structures obtained by solution methods, with inclusion of peptoid‐based structures and the complementary roles of polymerizations and step‐by‐step synthetic methods. Moreover, we describe relationships between naturally occurring peptide‐based structures, such as Geobacter pili, that in turn inspire self‐assembly of peptide‐based structures, composites with polymer materials, and assemblies therefrom.

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High‐Throughput Screening of pH‐Dependent β‐sheet Self‐Assembling Peptide

Ye,

Tian,

Han

et al. 2024

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AbstractpH‐dependent peptide biomaterials hold tremendous potential for cell delivery and tissue engineering. However, identification of responsive self‐assembling sequences with specified secondary structure remains a challenge. In this work, An experimental procedure based on the one‐bead one‐compound (OBOC) combinatorial library is developed to rapidly screen self‐assembling β‐sheet peptides at neutral aqueous solution (pH 7.5) and disassemble at weak acidic condition (pH 6.5). Using the hydrophobic fluorescent molecule thioflavin T (ThT) as a probe, resin beads displaying self‐assembling peptides show fluorescence under pH 7.5 due to the insertion of ThT into the hydrophobic domain, and are further cultured in pH 6.5 solution. The beads with extinguished fluorescence are selected. Three heptapeptides are identified that can self‐assemble into nanofibers or nanoparticles at pH 7.5 and disassemble at pH 6.5. P1 (LVEFRHY) shows a rapid acid response and morphology transformation with pH modulation. Changes in the charges of histidine and hydrophobic phenyl motif of phenylalanine may play important roles in the formation of pH‐responsive β‐sheet nanofiber. This high‐throughput screening method provides an efficient way to identify pH‐dependent β‐sheet self‐assembling peptide and gain insights into structural design of such nanomaterials.

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Self‐assembling Peptides with Internal Ionizable Unnatural Amino Acids: A General Approach to pH‐responsive Peptide Materials

Cited by 3 publications

References 62 publications

In Situ Synthesis and Self-Assembly of Peptide–PEG Conjugates: A Facile Method for the Construction of Fibrous Hydrogels

In Situ Synthesis and Self-Assembly of Peptide–PEG Conjugates: A Facile Method for the Construction of Fibrous Hydrogels

Building structured, functional materials inspired by nature: Using peptides, peptoids, and polymerizations

High‐Throughput Screening of pH‐Dependent β‐sheet Self‐Assembling Peptide

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