Cited by 170Antimicrobial Peptides and ActivitiesAntimicrobial agents and applicationsChemical Synthesis and Analysis

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Cathelicidin family of antimicrobial peptides: proteolytic processing and protease resistance

Shinnar, Ann Eisenberg, Butler, Kathryn L., Park, Hyon Ju·2003·Bioorganic Chemistry

DOI 10.1016/s0045-2068(03)00080-4

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Abstract

Cathelicidins are a gene family of antimicrobial peptides produced as inactive precursors. Signal peptidase removes the N-terminal signal sequence, while peptidylglycine alpha-amidating monooxygenase often amidates and cleaves the C-terminal region. Removal of the cathelin domain liberates the active antimicrobial peptide. For mammalian sequences, this cleavage usually occurs through the action of elastase, but other tissue-specific processing enzymes may also operate. Once released, these bioactive peptides are susceptible to proteolytic degradation. We propose that some mature cathelicidins are naturally resistant to proteases due to their unusual primary structures. Among mammalian cathelicidins, proline-rich sequences should resist attack by serine proteases because proline prevents cleavage of the scissile bond. In hagfish cathelicidins, the unusual amino acid bromotryptophan may make the active peptides less susceptible to proteolysis for steric reasons. Such protease resistance could extend the pharmacokinetic lifetimes of cathelicidins in vivo, sustaining antimicrobial activity.

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Authors: Shinnar, A. E., Butler, K. L., & Park, H. J.
Affiliations: Columbia University (US)
Corresponding author: Shinnar, Ann Eisenberg
Venue: Bioorganic Chemistry
Publisher: Elsevier BV
Published: 2003-12
Volume: 31
Issue: 6
Pages: 425-436
ISSN: 0045-2068 (ISSN-L)
DOI: 10.1016/s0045-2068(03)00080-4
OpenAlex: W1966733674
Cited by: 170
References: 50
Citations by year: 2026: 5 · 2025: 6 · 2024: 12 · 2023: 11 · 2022: 3 · 2021: 9 · 2020: 5 · 2019: 6 · 2018: 8 · 2017: 5 · 2016: 9 · 2015: 11 · 2014: 14 · 2013: 10 · 2012: 4
FWCI: 3.87
Type: journal article
Language: en
Open access: closed
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
Locations: Bioorganic Chemistry (publishedVersion)
PubMed (publishedVersion)
Topics: Life Sciences › Immunology and Microbiology › Microbiology › Antimicrobial Peptides and Activities
Life Sciences › Immunology and Microbiology › Applied Microbiology and Biotechnology › Antimicrobial agents and applications
Physical Sciences › Chemistry › Organic Chemistry › Chemical Synthesis and Analysis
Keywords: cathelicidin, antimicrobial peptides, proteolytic processing, protease resistance, signal peptidase, peptidylglycine alpha-amidating monooxygenase, proline-rich sequences, serine protease, pharmacokinetics
MeSH terms: Amino Acid Sequence, Animals, Arginine, Binding Sites, Multigene Family, Hagfishes, Humans, Mixed Function Oxygenases, Molecular Sequence Data, Multienzyme Complexes, Endopeptidases, Proline, Proteins, Tryptophan, Cysteine Proteinase Inhibitors, Sequence Homology, Amino Acid, Protein Sorting Signals, Antimicrobial Cationic Peptides, Cathelicidins

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Cathelicidin family of antimicrobial peptides: proteolytic processing and protease resistance

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