ArticleBiochemical and biophysical research communications2020
Incorporation of α-methylated amino acids into Apolipoprotein A-I mimetic peptides improves their helicity and cholesterol efflux potential.
Article in Biochemical and biophysical research communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
7 citing papers in PubMed, 9 citations in OpenAlex.
- α-Alkylated α-amino acids reduce the aggregation of unfolded peptides.RSC advances · 2026Article
- Interplay between CChembiochem : a European journal of chemical biology · 2025Article
- Therapeutic peptides for coronary artery diseases: in silico methods and current perspectives.Amino acids · 2024Review
- Systemic consequences of abnormal cholesterol handling: Interdependent pathways of inflammation and dyslipidemia.Frontiers in immunology · 2022Review
- Development of CHARMM Additive Potential Energy Parameters for α-Methyl Amino Acids.The journal of physical chemistry. B · 2021Article
- Apolipoprotein mimetics in cancer.Seminars in cancer biology · 2021Review
- Review
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 1 country.
Funding
Abstract
Apolipoprotein A-I (ApoA-I) mimetic peptides are potential therapeutic agents for promoting the efflux of excess cellular cholesterol, which is dependent upon the presence of an amphipathic helix. Since α-methylated Ala enhances peptide helicity, we hypothesized that incorporating other types of α-methylated amino acids into ApoA-I mimetic peptides may also increase their helicity and cholesterol efflux potential. The last helix of apoA-I, peptide 'A' (VLESFKVSFLSALEEYTKKLNT), was used to design peptides containing a single type of α-methylated amino acid substitution (Ala/A
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Registered trials
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