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2020
DOI: 10.1016/j.csbj.2020.07.015
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Novel zwitterionic vectors: Multi-functional delivery systems for therapeutic genes and drugs

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Cited by 60 publications
(45 citation statements)
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References 198 publications
(253 reference statements)
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“…FTIR spectroscopy was used to detect changes in the characteristic bands of GONPs and after GONPs–PEG coupling. In general, amino acids are zwitterions that have spectra that contain both primary amine and carboxylate functional groups [ 22 ]. Figure 4 shows the FTIR spectrum of GONPs; the peaks at 3338 cm −1 are stretching related to OH, while 1618, 1382, and 1026 cm −1 are C=O groups in carbonyl [-C(=O)-] and carboxyl (-COOH) and these results are consistent with a previous study published by Charmi J et al [ 23 ].…”
Section: Resultsmentioning
confidence: 99%
“…FTIR spectroscopy was used to detect changes in the characteristic bands of GONPs and after GONPs–PEG coupling. In general, amino acids are zwitterions that have spectra that contain both primary amine and carboxylate functional groups [ 22 ]. Figure 4 shows the FTIR spectrum of GONPs; the peaks at 3338 cm −1 are stretching related to OH, while 1618, 1382, and 1026 cm −1 are C=O groups in carbonyl [-C(=O)-] and carboxyl (-COOH) and these results are consistent with a previous study published by Charmi J et al [ 23 ].…”
Section: Resultsmentioning
confidence: 99%
“…Electrostatic interactions have a great influence on the conformation of the peptides. , Understanding the relationship between a peptide’s sequence and structure has always been a challenging task, even though this has been a focus of theoretical research for half a century. Zwitterionic peptides, carrying opposite charge groups located on different segment units, are one class of representatives with research prospects and broad applications such as antifouling, biolubrication, and drug delivery. The antifouling properties of zwitterionic peptides come from the hydration of the charge groups and the conformations of the surface-tethered peptides. The charge distribution of the peptides can significantly affect their conformation and functionality. Thus, it is of great significance to understand the relationship between charge sequence and the assembly behavior of zwitterionic peptides.…”
Section: Introductionmentioning
confidence: 99%
“…Amino acids are zwitterionic compounds capable of forming negatively charged carboxylates and positively charged ammonium groups in aqueous systems of neutral pH. 41,42 There are only a few studies conducted regarding the utilization of amino acids for enhancing the antifouling characteristic of membranes, 43–45 while there is only one credible report on nanoparticle modification by zwitterionic compounds for use in thin-film nanocomposite FO membranes, which is indeed published by our research team recently. 46 Thus, to elucidate the influence of the zwitterion-functionalized nanomodifier on the desalination and antifouling performance, particularly the elimination of metallic ions of FO membranes, herein, we have reported the zwitter ionization of MIL-125-NH 2 MOF by cysteine amino acid and exploited it as a modifier in the polyethersulfone/polyamide (PES/PA) thin-film composite membrane.…”
Section: Introductionmentioning
confidence: 99%