Interaction Analyses of Amyloid β Peptide (1–40) with Glycosaminoglycan Model Polymers

Miura, Yoshiko; Mizuno, H.

doi:10.1246/bcsj.20100094

Cited by 25 publications

(20 citation statements)

References 27 publications

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“…Miura and coworkers found that lower molecular weight heparin mimics were able to inhibit amyloid-beta aggregation better than the higher molecular weight heparin mimics. 25 …”

Section: Introductionmentioning

confidence: 99%

Structure activity relationship of heparin mimicking polymer p(SS-co-PEGMA): effect of sulfonation and polymer size on FGF2-receptor binding

Paluck

Maynard

2017

Polym. Chem.

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Fibroblast growth factor-2 (FGF2) is a heparin binding protein that plays a role in a range of biological functions such as wound healing and bone regeneration. Heparin, a highly sulfated glycosaminoglycan, is required for FGF2 to bind to its receptor. Therefore, polymeric mimics of heparin are widely studied for their ability to manipulate FGF2-induced biological interactions. It is known that altering the degree of sulfonated monomer incorporation and size of heparin-mimicking polymers can affect protein-receptor binding. To elucidate the relationship between degree of sulfonation and receptor binding for the heparin-mimicking polymer, poly(styrene sulfonate-co-poly(ethylene glycol) methyl ether methacrylate) (p(SS-co-PEGMA)) a library was synthesized to contain nine polymers with degrees of sulfonation ranging from 0-100%. Kinetics of the polymerization was evaluated and reactivity ratios compared to literature results. These polymers were then tested for their ability to enhance FGF2 binding with its receptor as both covalent conjugates and as excipients. In a receptor based enzyme-linked immunosorbant assay (ELISA), as well as a cell-based study, the polymer with 81% SS incorporation enhanced receptor binding compared to FGF2 alone, and to a greater extent than the other polymers. Therefore, another library of polymers was prepared maintaining the degree of sulfonation at 81% and changing the size from 41 to 390 monomer repeat units. The polymers were again tested in receptor based ELISA and cell studies, and all of the different sizes performed similarly, except for degree of polymerization 295 and 390, which had reduced response in the cellular assay. These results provide important information for the use of pSS-co-PEGMA as a potential heparin-mimicking therapeutic.

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“…Miura and coworkers found that lower molecular weight heparin mimics were able to inhibit amyloid-beta aggregation better than the higher molecular weight heparin mimics. 25 …”

Section: Introductionmentioning

confidence: 99%

Structure activity relationship of heparin mimicking polymer p(SS-co-PEGMA): effect of sulfonation and polymer size on FGF2-receptor binding

Paluck

Maynard

2017

Polym. Chem.

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“…No noticeable changes in the peptide structure were observed upon peptide/heparin complex formation. However, a weaker intensity of CD bands of bound ECL2 and Nt, which was also seen for other heparin‐binding peptides, can indicate their strong interaction with the glycosaminoglycan . Since the addition of HFIP does not influence the conformation of heparin, it was possible to evaluate the conformational changes in the peptides upon heparin binding by the subtraction of its CD spectrum from the CD spectra of the complexes (Figure B and 2C).…”

Section: Resultsmentioning

confidence: 98%

Modeling interaction between gp120 HIV protein and CCR5 receptor

Guryanov

Real‐Fernández

Sabatino

et al. 2019

Journal of Peptide Science

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The study of the process of HIV entry into the host cell and the creation of biomimetic nanosystems that are able to selectively bind viral particles and proteins is a high priority research area for the development of novel diagnostic tools and treatment of HIV infection. Recently, we described multilayer nanoparticles (nanotraps) with heparin surface and cationic peptides comprising the N-terminal tail (Nt) and the second extracellular loop (ECL2) of CCR5 receptor, which could bind with high affinity some inflammatory chemokines, in particular, Rantes. Because of the similarity of the binding determinants in CCR5 structure, both for chemokines and gp120 HIV protein, here we expand this approach to the study of the interactions of these biomimetic nanosystems and their components with the peptide representing the V3 loop of the activated form of gp120. According to surface plasmon resonance results, a conformational rearrangement is involved in the process of V3 and CCR5 fragments binding. As in the case of Rantes, ECL2 peptide showed much higher affinity to V3 peptide than Nt (K D = 3.72 × 10 −8 and 1.10 × 10 −6 M, respectively). Heparin-covered nanoparticles bearing CCR5 peptides effectively bound V3 as well. The presence of both heparin and the peptides in the structure of the nanotraps was shown to be crucial for the interaction with the V3 loop. Thus, short cationic peptides ECL2 and Nt proved to be excellent candidates for the design of CCR5 receptor mimetics.

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“…The second step of the synthesis, the coupling between 1a and b and acryloyl chloride, was also conducted in aqueous solution without isolating 1a and b . The amino group selectively reacted with acryloyl chloride in aqueous solution because the nucleophilicity of amino group was higher than those of hydroxy group and water . After the first step reaction, the reaction mixture was washed with chloroform to thoroughly extract excess 4‐aminobenzentiol and was directly added with acryloyl chloride to yield 2a and b (Table ).…”

Section: Resultsmentioning

confidence: 99%

Protecting-group-free synthesis of glycopolymers bearing thioglycosides via one-pot monomer synthesis from free saccharides

Tanaka

Inoue

Shoda

et al. 2014

J. Polym. Sci. Part A: Polym. Chem.

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Polyacrylamides having pendant thioglycosides were successfully synthesized from thioglycosidic monomers that were readily prepared by one‐pot method without any protection of the hydroxy groups on the starting free saccharides. The glycomonomers were synthesized by the direct synthesis of thioglycosides using 2‐chloro‐1,3‐dimethylimidazolinium chloride and 4‐aminobenzentiol, and the following acrylamidation. They were co‐polymerized with acrylamide into glycopolymers by reversible addition‐fragmentation chain transfer polymerization using a trithiocarbonate derivative as a chain transfer agent. The gold nanoparticles and gold‐coated quartz crystal microbalance sensor immobilized with the thiol‐terminated glycopolymers exhibited high affinity for the corresponding lectins due to multivalent interaction between saccharides and protein in aqueous solution. © 2014 Wiley Periodicals, Inc. J. Polym. Sci., Part A: Polym. Chem. 2014, 52, 3513–3520

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Interaction Analyses of Amyloid β Peptide (1–40) with Glycosaminoglycan Model Polymers

Cited by 25 publications

References 27 publications

Structure activity relationship of heparin mimicking polymer p(SS-co-PEGMA): effect of sulfonation and polymer size on FGF2-receptor binding

Structure activity relationship of heparin mimicking polymer p(SS-co-PEGMA): effect of sulfonation and polymer size on FGF2-receptor binding

Modeling interaction between gp120 HIV protein and CCR5 receptor

Protecting-group-free synthesis of glycopolymers bearing thioglycosides via one-pot monomer synthesis from free saccharides

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