Helical Antimicrobial Sulfono-γ-AApeptides

Li, Yaqiong; Wu, Haifan; Teng, P. K.; Bai, Ge; Lin, Xiaoyang; Zuo, Xiaobing; Cao, Chuanhai; Cai, Jianfeng

doi:10.1021/acs.jmedchem.5b00537

Cited by 62 publications

(78 citation statements)

References 38 publications

(93 reference statements)

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“…The results show that they can mimic HDPS and exhibit broad-spectrum activ- A helical scaffold of γ9 is also shown, in which red dots represent hydrophobic groups, and blue dots represent hydrophilic groups. Data taken from [37][38][39][40][41][42][43].…”

Section: γ-Aapeptides As Antimicrobial Agentsmentioning

confidence: 99%

“…Based on the abovementioned hypothesis and structural model, these sulfono-γ-AApeptides were designed with distinct amphipathicity, length and hydrophobicity, in order to understand the structure-function relationship existing in this class of foldamer for antimicrobial application (Figure 4 & Table 1) [42]. X-ray crystallography and 2D-NMR [49] analysis suggested that sulfono-γ-AApeptides form stable helical structures in solution.…”

Section: Helical Antimicrobial Sulfono-γ-aapeptidesmentioning

confidence: 99%

“…As expected, sequence γ9 shows significant antimicrobial activity. Although some sequences have same cationic charges and hydrophobic groups, their different location on the helical scaffold affects antimicrobial activity, as the distances between two adjacent side chains are not always the same on the sulfono-γ-AApeptides helical scaffold compared with side chains in α-helix [42]. In addition, small-angle x-ray scattering (SAXS) studies [52,53] shows the acetylation of N-terminus of the sequences significantly promote the folding of the sequences, and highly dense positive charges destabilize the helical folding [37,54].…”

Section: Helical Antimicrobial Sulfono-γ-aapeptidesmentioning

confidence: 99%

“…Furthermore, time-kill and fluorescence microscopy studying suggest that similar to HDPs, the sequence γ9 kill both Grampositive and Gram-negative bacteria via compromising their membranes. Finally, it should also be noted that sulfono-γ-AApeptides are highly resistant to enzyme degradation [42], augmenting their potential a ntimicrobial applications.…”

Section: Helical Antimicrobial Sulfono-γ-aapeptidesmentioning

confidence: 99%

“…In addition, they also harness immune response and inhibit lipopolysaccharide (LPS)-activated Toll-like receptor 4 (TLR4) signaling [36]. In addition, γ-AApeptides have shown promise as potential antimicrobial agents [37][38][39][40][41][42][43]. Recently, γ-AApeptides exhibit comparable or enhanced performance compared with ciprofloxacin in the prevention of biofilm formation of both Gram-positive and Gram-negative bacteria [44].…”

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The Development of Antimicrobial γ-Aapeptides

et al. 2016

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Host-defense peptides (HDPs) are promising next generation of antibiotic agents, as they have the potential to circumvent emerging drug resistance, due to their mechanism of bacterial killing through disruption of their membranes. Nonetheless, HDPs have intrinsic drawbacks such as low-to-moderate activity, susceptibility to enzymatic degradation. In the past few years, we developed a new class of peptidomimetics named ‘γ-AApeptides’, which have superior resistance to proteolysis and a variety of diversification via straightforward synthesis. Our recent studies suggested that γ-AApeptides can mimic the bactericidal mechanism of HDPs and show potent and broad-spectrum activity against both Gram-positive and Gram-negative multidrug-resistant bacteria. In this review, we summarize our current studies of antimicrobial γ-AApeptides and discuss their potential future development as antimicrobial peptidomimetics.

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Section: γ-Aapeptides As Antimicrobial Agentsmentioning

confidence: 99%

Section: Helical Antimicrobial Sulfono-γ-aapeptidesmentioning

confidence: 99%

Section: Helical Antimicrobial Sulfono-γ-aapeptidesmentioning

confidence: 99%

Section: Helical Antimicrobial Sulfono-γ-aapeptidesmentioning

confidence: 99%

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Helical Foldamers from Aromatic Polymers

Zhang

Wang

2017

Encyclopedia of Polymer Science and Technology

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Foldamers are synthetic linear molecules or macromolecules that adopt confined conformations induced by noncovalent forces. Conjugated polymers have relatively high rigidity. They can be induced by noncovalent interactions to fold into well‐predictable helical conformations. Backbones that have been developed for the formation of such polymeric helices include those composed of m ‐arylene ethynylene, aromatic amide, hydrazide, urea, trizole, and axodiazole segments. Noncovalent interactions typically used as driving forces for the formation of such helical conformations include solvophobicity and intra‐ and/or intermolecular hydrogen bonding. In general, polymeric foldamers possess a tubular cavity with a well‐defined diameter. Their length or depth is defined by the degree of polymerization. Such polymeric foldamers are conformationally dynamic and can exhibit unique twist‐sense bias tuned by side‐chain chirality or by chiral guest induction. Moreover, such hollow unimacromolecular helices can function as efficient tubular receptors for discrete guests and as transmembrane channels for transporting different ions. This article summarizes the studies of helical foldamers formed by aromatic polymers and their properties and functions.

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Antimicrobial Guanidinylate Polycarbonates Show Oral In Vivo Efficacy Against Clostridioides Difficile

Xue,

Chakraborty,

Gao

et al. 2024

Adv Healthcare Materials

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The emerging antibiotic resistance has been named by the World Health Organization (WHO) as one of the top 10 threats to public health. Notably, methicillin‐resistant Staphylococcus aureus (MRSA) and vancomycin‐resistant Enterococcus faecalis (VREF) are designated as serious threats, whereas Clostridioides difficile (C. difficile) is recognized as one of the most urgent threats to human health and unmet medical need. Among different strategies to combat these bacteria, host‐defense peptide (HDP) – mimicking polymer materials are found to be versatile and promising. However, the vast majority of antibiotic polymer applications were limited to topical application due to their potential systematic toxicity. Herein, we report the design and application of novel biodegradable polymers – the lipidated antimicrobial guanidinylate polycarbonates. These polymers showed potent antimicrobial activity against a panel of Gram‐negative and Gram‐positive bacteria with fast‐killing kinetics and low resistance development tendency. The mechanism of the bacterial killing process was investigated, which suggested that the antimicrobial activity of the polymer was mainly due to bacterial membrane disruption, analogous to that of HDPs. More importantly, the optimal polymer showed excellent antibacterial activity against C. difficile infection (CDI) in vivo via oral administration, which is very unusual as polymer applications are generally limited to injection. In addition, compared with vancomycin, the standard drug for the treatment of CDI but suffers from short protective efficacy and a high relapse rate, the polymer demonstrated a much‐prolonged therapeutic effect and virtually diminished recurrence rate of CDI. The convenient synthesis, easy scale‐up, low cost, as well as biodegradability of this class of polycarbonates, together with their in vitro broad‐spectrum antimicrobial activity and orally in vivo efficacy against CDI, suggest the great potential of lipidated guandinylate polycarbonates as a new class of antibacterial biomaterials to treat CDI and combat emerging antibiotic resistance.This article is protected by copyright. All rights reserved

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Helical Antimicrobial Sulfono-γ-AApeptides

Cited by 62 publications

References 38 publications

The Development of Antimicrobial γ-Aapeptides

The Development of Antimicrobial γ-Aapeptides

Helical Foldamers from Aromatic Polymers

Antimicrobial Guanidinylate Polycarbonates Show Oral In Vivo Efficacy Against Clostridioides Difficile

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