Zwitterionic polypeptides bearing carboxybetaine and sulfobetaine: synthesis, self-assembly, and their interactions with proteins

Tsai, Yu Lin; Tseng, Yu-Chao; Chen, Yan Miao; Wen, Tain Ching; Jan, Jeng‐Shiung

doi:10.1039/c7py01167a

Cited by 25 publications

(11 citation statements)

References 66 publications

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“…The results suggested all the hydrogel samples self-assembled to form ill-defined three-dimensional (3D) nano-assemblies. In the sol state, all the samples except 3 s -PLL 22 - b -PLeu 5.5 formed two-dimensional (2D) nano-assemblies [ 47 , 48 ]. Rather, 3 s -PLL 22 - b -PLeu 5.5 self-assembled to form one-dimensional (1D) fibrillar morphology, analogous to the study by Pine et al, showing that of the linear PLL- b -PLeu polypeptide hydrogels comprised of 1D twisted fibrils [ 33 ].…”

Section: Resultsmentioning

confidence: 99%

Polypeptide Composition and Topology Affect Hydrogelation of Star-Shaped Poly(L-lysine)-Based Amphiphilic Copolypeptides

Phan

Huang

Tsai

et al. 2021

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In this research, we studied the effect of polypeptide composition and topology on the hydrogelation of star-shaped block copolypeptides based on hydrophilic, coil poly(L-lysine)20 (s-PLL20) tethered with a hydrophobic, sheet-like polypeptide segment, which is poly(L-phenylalanine) (PPhe), poly(L-leucine) (PLeu), poly(L-valine) (PVal) or poly(L-alanine) (PAla) with a degree of polymerization (DP) about 5. We found that the PPhe, PLeu, and PVal segments are good hydrogelators to promote hydrogelation. The hydrogelation and hydrogel mechanical properties depend on the arm number and hydrophobic polypeptide segment, which are dictated by the amphiphilic balance between polypeptide blocks and the hydrophobic interactions/hydrogen bonding exerted by the hydrophobic polypeptide segment. The star-shaped topology could facilitate their hydrogelation due to the branching chains serving as multiple interacting depots between hydrophobic polypeptide segments. The 6-armed diblock copolypeptides have better hydrogelation ability than 3-armed ones and s-PLL-b-PPhe exhibits better hydrogelation ability than s-PLL-b-PVal and s-PLL-b-PLeu due to the additional cation–π and π–π interactions. This study highlights that polypeptide composition and topology could be additional parameters to manipulate polypeptide hydrogelation.

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Section: Resultsmentioning

confidence: 99%

Polypeptide Composition and Topology Affect Hydrogelation of Star-Shaped Poly(L-lysine)-Based Amphiphilic Copolypeptides

Phan

Huang

Tsai

et al. 2021

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“…In contrast to the neutral polymers, proteins bind electrostatically to charged polyelectrolytes. − Such complexes have been used to stabilize proteins against aggregation, denaturation, or biochemical degradation. − A limited number of studies of poly(zwitterion) interactions with proteins reported that poly(zwitterions) can inhibit antibody binding or substrate recognition, suggesting a direct protein–polymer association . In other studies, the polymers reportedly repel proteins such as BSA or lysozyme . Tethered zwitterionic chains also reportedly stabilize proteins. , These seemingly contradictory findings highlight the need for quantitative methods to establish the effect of poly(zwitterions) on protein stability and thermal denaturation.…”

Section: Introductionmentioning

confidence: 99%

Soluble Zwitterionic Poly(sulfobetaine) Destabilizes Proteins

et al. 2018

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The widespread interest in neutral, water-soluble polymers such as poly(ethylene glycol) (PEG) and poly(zwitterions) such as poly(sulfobetaine) (pSB) for biomedical applications is due to their widely assumed low protein binding. Here we demonstrate that pSB chains in solution can interact with proteins directly. Moreover, pSB can reduce the thermal stability and increase the protein folding cooperativity relative to proteins in buffer or in PEG solutions. Polymer-dependent changes in the tryptophan fluorescence spectra of three structurally-distinct proteins reveal that soluble, 100 kDa pSB interacts directly with all three proteins and changes both the local polarity near tryptophan residues and the protein conformation. Thermal denaturation studies show that the protein melting temperatures decrease by as much as ∼1.9 °C per weight percent of polymer and that protein folding cooperativity increases by as much as ∼130 J mol K per weight percent of polymer. The exact extent of the changes is protein-dependent, as some proteins exhibit increased stability, whereas others experience decreased stability at high soluble pSB concentrations. These results suggest that pSB is not universally protein-repellent and that its efficacy in biotechnological applications will depend on the specific proteins used.

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“…The self-assembled nanostructures of the polypeptide hydrogels (8.0 wt%) were characterized by small-angle X-ray scattering (SAXS) analysis ( Figure 4 ). For all hydrogel samples, the scattering intensity ( I ) exhibited a relation of I ( q ) ∝ q −n with n = 3.2–3.8, indicating the network forming 3D assembled nanostructures with ill-defined morphology [ 38 , 39 ]. The SAXS data were fitted by SasView software to compute the radius of gyration (R g ) of nano-assemblies formed by the packing of the grafted moieties.…”

Section: Resultsmentioning

confidence: 99%

Synthesis and Hydrogelation of Star-Shaped Graft Copolypetides with Asymmetric Topology

Phan

Yang

Tsai

et al. 2022

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To study the self-assembly and hydrogel formation of the star-shaped graft copolypeptides with asymmetric topology, star-shaped poly(L-lysine) with various arm numbers were synthesized by using asymmetric polyglycerol dendrimers (PGDs) as the initiators and 1,1,3,3-tetramethylguanidine (TMG) as an activator for OH groups, followed by deprotection and grafting with indole or phenyl group on the side chain. The packing of the grafting moiety via non-covalent interactions not only facilitated the polypeptide segments to adopt more ordered conformations but also triggered the spontaneous hydrogelation. The hydrogelation ability was found to be correlated with polypeptide composition and topology. The star-shaped polypeptides with asymmetric topology exhibited poorer hydrogelation ability than those with symmetric topology due to the less efficient packing of the grafted moiety. The star-shaped polypeptides grafted with indole group on the side chain exhibited better hydrogelation ability than those grafted with phenyl group with the same arm number. This report demonstrated that the grafted moiety and polypeptide topology possessed the potential ability to modulate the polypeptide hydrogelation and hydrogel characteristics.

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Zwitterionic polypeptides bearing carboxybetaine and sulfobetaine: synthesis, self-assembly, and their interactions with proteins

Abstract: Zwitterionic polypeptides bearing carboxybetaine and sulfobetaine were synthesized and their self-assembly and protein interactions were evaluated.

Cited by 25 publications

References 66 publications

Polypeptide Composition and Topology Affect Hydrogelation of Star-Shaped Poly(L-lysine)-Based Amphiphilic Copolypeptides

Polypeptide Composition and Topology Affect Hydrogelation of Star-Shaped Poly(L-lysine)-Based Amphiphilic Copolypeptides

Soluble Zwitterionic Poly(sulfobetaine) Destabilizes Proteins

Synthesis and Hydrogelation of Star-Shaped Graft Copolypetides with Asymmetric Topology

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