ArticleProtein science : a publication of the Protein Society2020
Effects of histatin 5 modifications on antifungal activity and kinetics of proteolysis.
Article in Protein science : a publication of the Protein Society, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 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.
The trial behind it
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
21 citing papers in PubMed, 28 citations in OpenAlex.
- The journey of bioactive peptides in vivo: cutting-edge advances in absorption, transport, and bioavailability.Bioprocess and biosystems engineering · 2026Review
- Artificial Intelligence-Driven Antimicrobial Peptide Discovery: Prediction, Generation, Mining and Optimization.Probiotics and antimicrobial proteins · 2026Review
- Optimizing Histatin 5: Effects of K13 and K17 Substitutions on Proteolytic Stability and Antifungal Activity.Computational and structural biotechnology journal · 2026Article
- Exploring the Healing Powers of Histatins: From Oral Health to Therapeutics.International journal of molecular sciences · 2025Review
- Reducing Functional Domain of Histatin 5 Improves Antifungal Activity and Prevents Proteolytic Degradation.Microorganisms · 2025Article
- Article
- Role of amino acid substitutions on proteolytic stability of histatin 5 in the presence of secreted aspartyl proteases and salivary proteases.Protein science : a publication of the Protein Society · 2025Article
- Secreted Aspartic Proteinases: Key Factors inInternational journal of molecular sciences · 2024Review
- Exploring therapeutic avenues: mesenchymal stem/stromal cells and exosomes in confronting enigmatic biofilm-producing fungi.Archives of microbiology · 2023Review
- Strategies and opportunities for engineering antifungal peptides for therapeutic applications.Current opinion in biotechnology · 2023Review
- Quantifying the Antifungal Activity of Peptides Against Candida albicans.Journal of visualized experiments : JoVE · 2023Article
- Antimicrobial peptides as drugs with double response againstFrontiers in microbiology · 2023Review
- Anti-Microbial Peptides: Strategies of Design and Development and Their Promising Wound-Healing Activities.Molecular biology reports · 2022Review
- Antimicrobial Peptides with Anti-International journal of molecular sciences · 2022Review
- Histatin 5 Metallopeptides and Their Potential againstBiomolecules · 2021Review
- Histatin 5 variant reduces Candida albicans biofilm viability and inhibits biofilm formation.Fungal genetics and biology : FG & B · 2021Article
- Membrane-Interacting Antifungal Peptides.Frontiers in cell and developmental biology · 2021Review
- Online capillary electrophoresis - mass spectrometry analysis of histatin-5 and its degradation products.The Analyst · 2020Article
- Bio- and Nanotechnology as the Key for Clinical Application of Salivary Peptide Histatin: A Necessary Advance.Microorganisms · 2020Review
- Effects of histatin 5 modifications on antifungal activity and kinetics of proteolysis.Protein science : a publication of the Protein Society · 2020Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
Abstract
Histatin 5 (Hst-5) is an antimicrobial peptide with strong antifungal activity against Candida albicans, an opportunistic pathogen that is a common cause of oral thrush. The peptide is natively secreted by human salivary glands and shows promise as an alternative therapeutic against infections caused by C. albicans. However, Hst-5 can be cleaved and inactivated by a family of secreted aspartic proteases (Saps) produced by C. albicans. Single-residue substitutions can significantly affect the proteolytic resistance of Hst-5 to Saps and its antifungal activity; the K17R substitution increases resistance to proteolysis, while the K11R substitution enhances antifungal activity. In this work, we showed that the positive effects of these two single-residue modifications can be combined in a single peptide, K11R-K17R, with improved proteolytic resistance and antifungal activity. We also investigated the effect of additional single-residue substitutions, with a focus on the effect of addition or removal of negatively charged residues, and found Sap-dependent effects on degradation. Both single- and double-substitutions affected the kinetics of proteolytic degradation of the intact peptide and of the fragments formed during degradation. Our results demonstrate the importance of considering proteolytic stability and not just antimicrobial activity when designing peptides for potential therapeutic applications.
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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.