ReviewBiopolymers2009
Intrinsic amino acid side-chain hydrophilicity/hydrophobicity coefficients determined by reversed-phase high-performance liquid chromatography of model peptides: comparison with other hydrophilicity/hydrophobicity scales.
Review in Biopolymers, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
What it found
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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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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
38 citing papers in PubMed, 120 citations in OpenAlex.
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- Context Dependency of Hydrophobicity in Intrinsically Disordered Proteins: Insights from a New Dewetting Free Energy-Based Hydrophobicity Scale.The journal of physical chemistry. B · 2025Article
- Impact of Excipient Extraction and Buffer Exchange on Recombinant Monoclonal Antibody Stability.Molecular pharmaceutics · 2024Article
- Conformational Space of the Translocation Domain of Botulinum Toxin: Atomistic Modeling and Mesoscopic Description of the Coiled-Coil Helix Bundle.International journal of molecular sciences · 2024Article
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- Integrating machine learning to advance epitope mapping.Frontiers in immunology · 2024Review
- Antimicrobial peptide 2K4L disrupts the membrane of multidrug-resistantFrontiers in microbiology · 2023Article
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- Solubility-Aware Protein Binding Peptide Design Using AlphaFold.Biomedicines · 2022Article
- A story of peptides, lipophilicity and chromatography - back and forth in time.RSC medicinal chemistry · 2022Review
- Antimicrobial peptides: A plausible approach for COVID-19 treatment.Expert opinion on drug discovery · 2022Review
- Solution NMR and racemic crystallography provide insights into a novel structural class of cyclic plant peptides.RSC chemical biology · 2021Article
- Trp-Containing Antibacterial Peptides Impair Quorum Sensing and Biofilm Development in Multidrug-ResistantFrontiers in microbiology · 2021Article
- The Impact of Halogenated Phenylalanine Derivatives on NFGAIL Amyloid Formation.Chembiochem : a European journal of chemical biology · 2020Article
- A Comprehensive Review on Current Advances in Peptide Drug Development and Design.International journal of molecular sciences · 2019Review
- De Novo Designed Amphipathic α-Helical Antimicrobial Peptides Incorporating Dab and Dap Residues on the Polar Face To Treat the Gram-Negative Pathogen, Acinetobacter baumannii.Journal of medicinal chemistry · 2019Article
- Synergistic Antibacterial Activity of Designed Trp-Containing Antibacterial Peptides in Combination With Antibiotics Against Multidrug-ResistantFrontiers in microbiology · 2019Article
- In Silico Prediction of Diffusion Interaction Parameter (kPharmaceutical research · 2018Article
- Systematic Moiety Variations of Ultrashort Peptides Produce Profound Effects on Self-Assembly, Nanostructure Formation, Hydrogelation, and Phase Transition.Scientific reports · 2017Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
An accurate determination of the intrinsic hydrophilicity/hydrophobicity of amino acid side-chains in peptides and proteins is fundamental in understanding many area of research, including protein folding and stability, peptide and protein function, protein-protein interactions and peptide/protein oligomerization, as well as the design of protocols for purification and characterization of peptides and proteins. Our definition of intrinsic hydrophilicity/hydrophobicity of side-chains is the maximum possible hydrophilicity/hydrophobicity of side-chains in the absence of any nearest-neighbor effects and/or any conformational effects of the polypeptide chain that prevent full expression of side-chain hydrophilicity/hydrophobicity. In this review, we have compared an experimentally derived intrinsic side-chain hydrophilicity/hydrophobicity scale generated from RP-HPLC retention behavior of de novo designed synthetic model peptides at pH 2 and pH 7 with other RP-HPLC-derived scales, as well as scales generated from classic experimental and calculation-based methods of octanol/water partitioning of Nalpha-acetyl-amino-acid amides or free energy of transfer of free amino acids. Generally poor correlation was found with previous RP-HPLC-derived scales, likely due to the random nature of the peptide mixtures in terms of varying peptide size, conformation and frequency of particular amino acids. In addition, generally poor correlation with the classical approaches served to underline the importance of the presence of a polypeptide backbone when generating intrinsic values. We have shown that the intrinsic scale determined here is in full agreement with the structural characteristics of amino acid side-chains.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.