ArticleScientific reports2022
Development of truncated elastin-like peptide analogues with improved temperature-response and self-assembling properties.
Article in Scientific reports, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 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
8 citing papers in PubMed.
- Integrative Peptide Drug Development: Chemical Engineering, AI-Driven Design, and Cell-Penetrating Peptides.Pharmaceutics · 2026Review
- Nanoparticle Clearance and New Horizons in Engineered Drug Delivery.Pharmaceutics · 2026Review
- Stepwise LCST-Type Phase Separation in Mixtures of Short-Chain Elastin-Like Peptides With Minimal Structural Differences.Biopolymers · 2026Article
- Biomimetic polymers and their characterization: toward sustainable materials using synthetic biology.Frontiers in chemistry · 2026Review
- Review
- Merging Natural Biopolymers with Supramolecular Chemistry: Emulating the Native Extracellular Matrix's Complexity.ACS nano · 2025Review
- Rational Engineering of a Brevinin-2 Peptide: Decoupling Potency from Toxicity Through C-Terminal Truncation and N-Terminal Chiral Substitution.Antibiotics (Basel, Switzerland) · 2025Article
- Exploring LCST- and UCST-like Behavior of Branched Molecules Bearing Repeat Units of Elastin-like Peptides as Side Components.Biomacromolecules · 2024Article
Corrections and comments
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Authors and funding
9 authors.
Funding
Abstract
Functional peptides, which are composed of proteinogenic natural amino acids, are expected to be used as biomaterials with minimal environmental impact. Synthesizing a functional peptide with a shorter amino acid sequence while retaining its function is a easy and economical strategy. Furthermore, shortening functional peptides helps to elucidate the mechanism of their functional core region. Truncated elastin-like peptides (ELPs) are peptides consisting of repetitive sequences, derived from the elastic protein tropoelastin, that show the thermosensitive formation of coacervates. In this study, to obtain shortened ELP analogues, we synthesized several (Phe-Pro-Gly-Val-Gly)
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