γ-AApeptides as a New Strategy for Therapeutic Development
Open accessAbstract
A new class of peptidomimetics termed as "γ-AApeptides" was recently developed by our group. Similar to other peptidomimetics, γ-AApeptides are resistant to proteolytic degradation, and possess limitless potential to introduce chemically diverse functional groups. γ-AApeptides have shown great promise in biomedical applications. In this article, we will review a few examples of γ-AApeptides with biological potential. Certain γ-AApeptides can permeate cell membranes and therefore they can be used as potential drug carrier. γ-AApeptides can also bind to HIV RNA with high specificity and affinity, suggesting their potential application as anti-HIV agents. Moreover, they can mimic host-defense peptides and display potent and broad-spectrum activity towards a range of drug-resistant bacterial pathogens. They are also potential anti-cancer agents. For instance, they have shown great promise in targeted imaging of tumor in mouse model, and they are also capable of disrupting p53/DNA interactions, and thus antagonize STAT3 signaling pathway. Recently, from combinatorial screening, γ-AApeptides are identified to inhibit Aβ peptide aggregation, and thus they can be developed into potential anti- Alzheimer’s disease agent.
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γ-AApeptides are a newly developed class of peptidomimetics.
“Another newly developed class of peptidomimetics are the “γ-AApeptides.”52”
From Current and Future Treatments in Alzheimer Disease: An Update (2020) · cites this paper as [52]
Compound γ-AA26 seems almost 100-fold as efficient as compound 18 of KLVFF in inhibiting aggregation of Aβ42.
“One of them, compound γ-AA26, seems almost 100-fold as efficient as the compound 18 of the KLVFF in the inhibition of the aggregation of Aβ42.52”
From Current and Future Treatments in Alzheimer Disease: An Update (2020) · cites this paper as [52]
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- Authors
- Nimmagadda, A., Shi, Y., & Cai, J.
- Affiliations
- University of South Florida (US)
- Corresponding author
- Cai, Jianfeng
- Venue
- Current Medicinal Chemistry
- Publisher
- Bentham Science Publishers Ltd.
- Published
- 2019-07-08
- Volume
- 26
- Issue
- 13
- Pages
- 2313-2329
- ISSN
- 0929-8673 (ISSN-L)
- PMC
- PMC5936681
- OpenAlex
- W2767430564
- Cited by
- 21
- References
- 58
- Citations by year
- 2026: 1 · 2025: 1 · 2024: 2 · 2023: 1 · 2022: 8 · 2021: 3 · 2020: 2 · 2019: 2 · 2018: 1
- FWCI
- 0.33
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Current Medicinal Chemistry (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Digital Commons - University of South Florida (University of South Florida) (submittedVersion)
- Funders
- National Institutes of Health (1R01GM112652-01A1)
- National Natural Science Foundation of China (1351265)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Chemical Synthesis and Analysis
- Physical Sciences › Materials Science › Biomaterials › Supramolecular Self-Assembly in Materials
- Health Sciences › Medicine › Oncology › Peptidase Inhibition and Analysis
- Keywords
- peptidomimetics, cell membrane permeation, drug carriers, anti-HIV agents, antibacterial activity, drug-resistant bacteria, anticancer agents, tumor imaging, STAT3 signaling, amyloid-beta aggregation, Alzheimer's disease
- MeSH terms
- Protein Conformation, alpha-Helical, Animals, Anti-Bacterial Agents, Antineoplastic Agents, Humans, Peptide Fragments, Peptides, Cyclic, Amyloid beta-Peptides, Anti-HIV Agents, Cell Line, Tumor, Protein Multimerization, Peptidomimetics
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