Poly(ornithine‐co‐arginine‐co‐glycine‐co‐aspartic Acid): Preparation via NCA Polymerization and its Potential as a Polymeric Tumor‐Penetrating Agent

Yu, Haiyang; Tang, Zhaohui; Zhang, Dawei; Song, Wantong; Duan, Taicheng; Gu, Jian; Chen, Xuesi

doi:10.1002/mabi.201500040

Cited by 4 publications

(2 citation statements)

References 51 publications

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“…Biodegradable polypeptides have potential for medical applications such as carriers for protein conjugates and use in drug delivery systems . Copolypeptides resemble natural proteins in properties such as their degradability by proteolytic enzymes. , However, amino acids in natural proteins are arranged in a well-defined sequence, which leads to characteristic functionalities and properties. Block copolypeptides are interesting for specific applications due to their ability to self-assemble .…”

Section: Introductionmentioning

confidence: 99%

Synthesis and Cell Interaction of Statistical l-Arginine–Glycine–l-Aspartic Acid Terpolypeptides

et al. 2018

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Copolymerizations and terpolymerizations of N-carboxyanhydrides (NCAs) of glycine (Gly), N-carbobenzyloxy-l-ornithine (Z-Orn), and β-benzyl-l-aspartate (Bz-Asp) were investigated. In situ H NMR spectroscopy was used to monitor individual comonomer consumptions during binary and ternary copolymerizations. The six relevant reactivity ratios were determined from copolymerizations of the NCAs of amino acids via nonlinear least-squares curve fitting. The reactivity ratios were subsequently used to maximize the occurrence of the Asp-Gly-Orn ( DGR') sequence in the terpolymers. Terpolymers with variable probability of occurrence of DGR' were prepared in the lab. Subsequently, the ornithine residues on the terpolymers were converted to l-arginine (R) residues via guanidination reaction after removal of the protecting groups. The resulting DGR terpolymers translate to traditional peptides and proteins with variable RGD content, due to the convention in nomenclature that peptides are depicted from N- to C-terminus, whereas the NCA ring-opening polymerization is conducted from C- to N-terminus. The l-arginine containing terpolymers were evaluated for cell interaction, where it was found that neuronal cells display enhanced adhesion and process formation when plated in the presence of statistical DGR terpolymers.

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Section: Introductionmentioning

confidence: 99%

Synthesis and Cell Interaction of Statistical l-Arginine–Glycine–l-Aspartic Acid Terpolypeptides

et al. 2018

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“…They found that due to the multiple chain folding of PGly, the lamellar structure of PBLG was stabilized. Finally, Yu et al [29] used poly(glycine) for synthesizing a polymeric tumor-penetrating agent.…”

Section: Introductionmentioning

confidence: 99%

Synthesis of Hybrid-Polypeptides m-PEO-b-poly(His-co-Gly) and m-PEO-b-poly(His-co-Ala) and Study of Their Structure and Aggregation. Influence of Hydrophobic Copolypeptides on the Properties of Poly(L-histidine)

et al. 2017

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Abstract:The highly diverse and sophisticated action of proteins results from their equally diverse primary structure, which along with the nature of interactions between the amino acids, defines the higher self-assembly of proteins. The interactions between amino acids can be very complicated, and their understanding is necessary in order to elucidate the protein structure-properties relationship. A series of well-defined hybrid-polypeptidic diblock copolymers of the type m-PEO-b-poly(His-co-Gly) and m-PEO-b-poly(His-co-Ala) was synthesized through the ring opening polymerization of the N-carboxyanhydrides of the corresponding amino acids, with a molar ratio of the hydrophobic peptide to histidine at 10%, 20% and 40%. The excellent purity of the monomers combined with the high vacuum techniques resulted in controlled polymerization with high molecular and compositional homogeneity. FT-IR, as well as circular dichroism, were employed to investigate the secondary structure of the polymers, while DLS, SLS and ζ-potential were utilized to study the aggregates formed in aqueous solutions, as well as their pH responsiveness. The results revealed that the randomly distributed monomeric units of glycine or alanine significantly influence L-histidine's structure. Depending on the pH, aggregates with a different structure, different molecular characteristics and a different surface charge are formed, potentially leading to very interesting bioapplications.

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Polypeptides Synthesized by Ring‐opening Polymerization of N‐Carboxyanhydrides

Yao

Zhou

Yan

2018

Bioinspired Materials Science and Engineering

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Poly(ornithine‐co‐arginine‐co‐glycine‐co‐aspartic Acid): Preparation via NCA Polymerization and its Potential as a Polymeric Tumor‐Penetrating Agent

Cited by 4 publications

References 51 publications

Synthesis and Cell Interaction of Statistical l-Arginine–Glycine–l-Aspartic Acid Terpolypeptides

Synthesis and Cell Interaction of Statistical l-Arginine–Glycine–l-Aspartic Acid Terpolypeptides

Synthesis of Hybrid-Polypeptides m-PEO-b-poly(His-co-Gly) and m-PEO-b-poly(His-co-Ala) and Study of Their Structure and Aggregation. Influence of Hydrophobic Copolypeptides on the Properties of Poly(L-histidine)

Polypeptides Synthesized by Ring‐opening Polymerization of N‐Carboxyanhydrides

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